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Conserved domains on  [gi|1358101401|ref|NP_945324|]
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MAP kinase-interacting serine/threonine-protein kinase 1 isoform 2 [Homo sapiens]

Protein Classification

MAP kinase-interacting serine/threonine-protein kinase 1( domain architecture ID 10197690)

MAP kinase-interacting serine/threonine-protein kinase 1 catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is phosphorylated and activated by p38 kinases and kinases in the Erk pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
34-322 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 664.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14174     1 DLYRLTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14174    81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFE 273
Cdd:cd14174   161 PITTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRGEVCRVCQNKLFE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14174   241 SIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
 
Name Accession Description Interval E-value
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
34-322 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 664.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14174     1 DLYRLTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14174    81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFE 273
Cdd:cd14174   161 PITTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRGEVCRVCQNKLFE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14174   241 SIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
41-321 4.83e-93

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 277.49  E-value: 4.83e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAG-HSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkKDRERILREIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKlnnsctpiTTPE 199
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---GHVKLADFGLARQLD--------PGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcQNKLFESIQEGK 279
Cdd:smart00220 153 LTTFVGTPEYMAPEVL-----LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ--------------LLELFKKIGKPK 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1358101401  280 YEFPDKDWaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:smart00220 214 PPFPPPEW-DISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
41-321 1.34e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.82  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-QAGHS-RSRVFREVETLYQCQGnKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKkDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDflhtkgiahrdlkpenilcespekvspvkicdfdlgsgmklnnsctpiTTP 198
Cdd:pfam00069  84 SLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------------------------------SGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcqNKLFESIQEG 278
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVL-----GGNPYGPKVDVWSLGCILYELLTGKPPFPGING---------------NEIYELIIDQ 175
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDKdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:pfam00069 176 PYAFPEL-PSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
36-317 1.97e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 169.04  E-value: 1.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:COG0515     9 YRIL-RLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADpeaRERFRREARALARLN-HPNIVRVYDVGEEDGRPYLVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGsgmklnnsc 192
Cdd:COG0515    87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL-TPDGR--VKLIDFGIA--------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELT---TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvcqn 269
Cdd:COG0515   155 RALGGATLTqtgTVVGTPGYMAPEQA-----RGEPVDPRSDVYSLGVTLYELLTGRPPFDGD-------SPAEL------ 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 270 klFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRL-SAAQVLQ 317
Cdd:COG0515   217 --LRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYqSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
41-323 7.19e-39

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 140.34  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsrvfrEVETLYQCQ---GNKNILE---------LIEFFEDDTRF 108
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKR----------EILKMKQVQhvaQEKSILMelshpfivnMMCSFQDENRV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKL 188
Cdd:PTZ00263   94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDF--GFAKKV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 nnsctpittPELT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVcrvc 267
Cdd:PTZ00263  169 ---------PDRTfTLCGTPEYLAPEVI-----QSKGHGKAVDWWTMGVLLYEFIAGYPPF---------FDDTPF---- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 268 qnKLFESIQEGKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSA-----AQVLQHPWVQG 323
Cdd:PTZ00263  222 --RIYEKILAGRLKFP--NW--FDGRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFHG 276
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
103-250 2.03e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.94  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 EDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICD 179
Cdd:NF033483   77 EDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL------ITKdgrVKVTD 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 180 FdlGSGMKLNNSCTPITTPELttpcGSAEYMAPEvvevftdQAT--FYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:NF033483  151 F--GIARALSSTTMTQTNSVL----GTVHYLSPE-------QARggTVDARSDIYSLGIVLYEMLTGRPPFDG 210
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
58-255 5.12e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 63.71  E-value: 5.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   58 QNGKEYAVKIIEKQAG---HSRSRVFREVETLYQCQgNKNILELIEFFE-DDTRFYLVFEKLQGGSILAHIQKQKHFNER 133
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPeeeHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  134 EASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLG---SGMKLNNSCTPITTPELTtpcGSAEYM 210
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGtllPGVRDADVATLTRTTEVL---GTPTYC 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1358101401  211 APEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLSGYPPFVGHCGAD 255
Cdd:TIGR03903  157 APEQLrgEPVTPNS-------DLYAWGLIFLECLTGQRVVQGASVAE 196
 
Name Accession Description Interval E-value
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
34-322 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 664.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14174     1 DLYRLTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14174    81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFE 273
Cdd:cd14174   161 PITTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRGEVCRVCQNKLFE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14174   241 SIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
34-321 0e+00

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 622.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14090     1 DLYKLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLN-NSC 192
Cdd:cd14090    81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKLSsTSM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLF 272
Cdd:cd14090   161 TPVTTPELLTPVGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDCGWDRGEACQDCQELLF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 273 ESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14090   241 HSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
34-321 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 561.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14173     1 DVYQLQEEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14173    81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNSDCS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFE 273
Cdd:cd14173   161 PISTPELLTPCGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWDRGEACPACQNMLFE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14173   241 SIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
36-320 4.15e-120

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 346.39  E-value: 4.15e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd05117     2 YEL-GKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKklKSEDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdlGSGMKLNNsct 193
Cdd:cd05117    80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDF--GLAKIFEE--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pitTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFE 273
Cdd:cd05117   155 ---GEKLKTVCGTPYYVAPEVLK-----GKGYGKKCDIWSLGVILYILLCGYPPFYGE---------------TEQELFE 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd05117   212 KILKGKYSFDSPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
41-321 4.83e-93

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 277.49  E-value: 4.83e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAG-HSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkKDRERILREIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKlnnsctpiTTPE 199
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---GHVKLADFGLARQLD--------PGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcQNKLFESIQEGK 279
Cdd:smart00220 153 LTTFVGTPEYMAPEVL-----LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ--------------LLELFKKIGKPK 213
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1358101401  280 YEFPDKDWaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:smart00220 214 PPFPPPEW-DISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
36-328 5.98e-88

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 266.47  E-value: 5.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTS--ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRsrvfrEVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14092     5 YELDLreEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSR-----EVQLLRLCQGHPNIVKLHEVFQDELHTYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGsgmKLNNSCT 193
Cdd:cd14092    80 LLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFA---RLKPENQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PittpeLTTPCGSAEYMAPEVVEVfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVCRvcqnKLFE 273
Cdd:cd14092   157 P-----LKTPCFTLPYAAPEVLKQ-ALSTQGYDESCDLWSLGVILYTMLSGQVPFQSP-------SRNESAA----EIMK 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQHN 328
Cdd:cd14092   220 RIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPS 274
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
43-322 7.65e-81

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 246.23  E-value: 7.65e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK----QAGHSRSrVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14007     8 LGKGKFGNVYLAREKKSGFIVALKVISKsqlqKSGLEHQ-LRREIEIQSHLR-HPNILRLYGYFEDKKRIYLILEYAPNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSctpittp 198
Cdd:cd14007    86 ELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADF--GWSVHAPSN------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVCRvcqnklfeSIQEG 278
Cdd:cd14007   154 RRKTFCGTLDYLPPEMVE-----GKEYDYKVDIWSLGVLCYELLVGKPPFESK-------SHQETYK--------RIQNV 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 279 KYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14007   214 DIKFPS----SVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
41-331 3.06e-79

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 243.69  E-value: 3.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14091     6 EEIGKGSYSVCKRCIHKATGKEYAVKIIDK----SKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPE-KVSPVKICDFDLGSGMKLNNSCtpittpe 199
Cdd:cd14091    82 LDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESgDPESLRICDFGFAKQLRAENGL------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGWDRGEVcrvcqnkLFESIQEGK 279
Cdd:cd14091   155 LMTPCYTANFVAPEVLK---KQG--YDAACDIWSLGVLLYTMLAGYTPF-----ASGPNDTPEV-------ILARIGSGK 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQgeQQHNGPD 331
Cdd:cd14091   218 IDLSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR--NRDSLPQ 267
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
36-320 3.70e-78

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 239.34  E-value: 3.70e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14003     2 YEL-GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSklKEEIEEKIKREIEIMKLLN-HPNIIKLYEVIETENKIYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFDLGSGMKLNNsc 192
Cdd:cd14003    80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILlDKNGN----LKIIDFGLSNEFRGGS-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 tpittpELTTPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKL 271
Cdd:cd14003   154 ------LLKTFCGTPAYAAPEVL-----LGRKYDgPKADVWSLGVILYAMLTGYLPFDDD---------------NDSKL 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 FESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14003   208 FRKILKGKYPIPS----HLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
36-320 2.75e-77

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 237.57  E-value: 2.75e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghSRSRvfREVETLYQCQGNKNILELIEFFE---DDTRFYL-V 111
Cdd:cd14089     2 YTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDN---PKAR--REVELHWRASGCPHIVRIIDVYEntyQGRKCLLvV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSgmkln 189
Cdd:cd14089    77 MECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAK----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nscTPITTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADC--GWDRgevcrvc 267
Cdd:cd14089   152 ---ETTTKKSLQTPCYTPYYVAPEVLG-----PEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspGMKK------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 268 qnklfeSIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14089   217 ------RIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
32-320 8.02e-76

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 234.17  E-value: 8.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKII--------EKQAGHSRSRVFREVETLYQCQGNKNILELIEFFE 103
Cdd:cd14093     1 FYAKYEP-KEILGRGVSSTVRRCIEKETGQEFAVKIIditgekssENEAEELREATRREIEILRQVSGHPNIIELHDVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDF--- 180
Cdd:cd14093    80 SPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VKISDFgfa 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 -DLGSGMKLNnsctpittpELttpCGSAEYMAPEVVEVFT-DQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgW 258
Cdd:cd14093   157 tRLDEGEKLR---------EL---CGTPGYLAPEVLKCSMyDNAPGYGKEVDMWACGVIMYTLLAGCPPF---------W 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 259 DRGevcrvcQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14093   216 HRK------QMVMLRNIMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
42-320 1.17e-72

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 225.67  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR-VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14095     7 VIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHmIENEVAILRRVK-HPNIVQLIEEYDTDTELYLVMELVKGGDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEKVSPVKICDFDLGsgmklnnscTPITTPe 199
Cdd:cd14095    86 FDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLvVEHEDGSKSLKLADFGLA---------TEVKEP- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGevcrvcQNKLFESIQEGK 279
Cdd:cd14095   156 LFTVCGTPTYVAPEILA-----ETGYGLKVDIWAAGVITYILLCGFPPFRSP-------DRD------QEELFDLILAGE 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14095   218 FEFLSPYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-320 4.01e-69

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 216.47  E-value: 4.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 111
Cdd:cd14083     2 RDKYEF-KEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKeDSLENEIAVLRKIK-HPNIVQLLDIYESKSHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgSGMKLNNS 191
Cdd:cd14083    80 MELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGL-SKMEDSGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpittpeLTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEvcrvcqNKL 271
Cdd:cd14083   159 --------MSTACGTPGYVAPEVLAQKP-----YGKAVDCWSIGVISYILLCGYPPF---------YDEND------SKL 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 FESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14083   211 FAQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
43-320 4.36e-67

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 210.84  E-value: 4.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREvetlyqcqgnKNILELIEF---------FEDDTRFYL 110
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVehtLNE----------RNILERVNHpfivklhyaFQTEEKLYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFDLGSGMKLN 189
Cdd:cd05123    71 VLDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILlDSDGH----IKLTDFGLAKELSSD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEvcrvcqn 269
Cdd:cd05123   147 GDRT-------YTFCGTPEYLAPEVL-----LGKGYGKAVDWWSLGVLLYEMLTGKPPFYAE-------NRKE------- 200
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 270 kLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRL---SAAQVLQHPW 320
Cdd:cd05123   201 -IYEKILKSPLKFPE----YVSPEAKSLISGLLQKDPTKRLgsgGAEEIKAHPF 249
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
41-328 4.94e-66

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 209.46  E-value: 4.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14166     9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIK-HENIVTLEDIYESTTHYYLVMQLVSGGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgSGMKLNNSctpittpeL 200
Cdd:cd14166    88 FDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGL-SKMEQNGI--------M 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEvcrvcqNKLFESIQEGKY 280
Cdd:cd14166   159 STACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVITYILLCGYPPF---------YEETE------SRLFEKIKEGYY 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 281 EFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQHN 328
Cdd:cd14166   219 EFESPFWDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGNTALH 266
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
43-323 1.76e-65

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 208.96  E-value: 1.76e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghsRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRM---EANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGGELLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGsgmklnnSCTPITTPELTT 202
Cdd:cd14180    91 RIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFA-------RLRPQGSRPLQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPevvEVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVCQNKLFESIQEGKYEF 282
Cdd:cd14180   164 PCFTLQYAAP---ELFSNQG--YDESCDLWSLGVILYTMLSGQVPFQS--------KRGKMFHNHAADIMHKIKEGDFSL 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 283 PDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd14180   231 EGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQG 271
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-321 1.03e-64

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 206.50  E-value: 1.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR--SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 111
Cdd:cd14086     1 DEYDLKEEL-GKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARdhQKLEREARICRLLK-HPNIVRLHDSISEEGFHYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNs 191
Cdd:cd14086    79 FDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQ- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpittPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGevcrvcQNKL 271
Cdd:cd14086   158 ------QAWFGFAGTPGYLSPEVL-----RKDPYGKPVDIWACGVILYILLVGYPPF---------WDED------QHRL 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 FESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14086   212 YAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWI 261
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-335 4.21e-64

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 205.27  E-value: 4.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghsRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14179    10 LKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRM---EANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGsgmklnnSCTPITT 197
Cdd:cd14179    87 GELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFA-------RLKPPDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVCRVCQnKLFESIQE 277
Cdd:cd14179   160 QPLKTPCFTLHYAAPELL-----NYNGYDESCDLWSLGVILYTMLSGQVPFQCH-------DKSLTCTSAE-EIMKKIKQ 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 278 GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQHNG-----PDALRS 335
Cdd:cd14179   227 GDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSnplmtPDILGS 289
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
32-326 5.55e-64

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 204.48  E-value: 5.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14178     1 FTDGYEI-KEDIGIGSYSVCKRCVHKATSTEYAVKIIDK----SKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CESPEKvspVKICDFDLGSGMK 187
Cdd:cd14178    76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILymdeSGNPES---IRICDFGFAKQLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSCtpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcGADcgwDRGEvcrvc 267
Cdd:cd14178   153 AENGL-------LMTPCYTANFVAPEVL-----KRQGYDAACDIWSLGILLYTMLAGFTPFAN--GPD---DTPE----- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 268 qnKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQ 326
Cdd:cd14178   211 --EILARIGSGKYALSGGNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREY 267
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
34-321 1.37e-63

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 202.53  E-value: 1.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIekqagHSRSRVFREVETLYQCQGNKNILELIEFFEDDTR----FY 109
Cdd:cd14172     3 DDYKLSKQVLGLGVNGKVLECFHRRTGQKCALKLL-----YDSPKARREVEHHWRASGGPHIVHILDVYENMHHgkrcLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQ--KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMK 187
Cdd:cd14172    78 IIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSctpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcRVC 267
Cdd:cd14172   158 VQNA--------LQTPCYTPYYVAPEVL-----GPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTG-----------QAI 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 268 QNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14172   214 SPGMKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
29-321 3.13e-63

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 201.85  E-value: 3.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  29 PGKFEDMYkLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRS------RVFREVETLYQCQgNKNILELIE 100
Cdd:cd14084     1 PKELRKKY-IMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRkfTIGSRReinkprNIETEIEILKKLS-HPCIIKIED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 101 FFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDF 180
Cdd:cd14084    79 FFDAEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 DLG------SGMKlnnsctpittpeltTPCGSAEYMAPEVVEVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCga 254
Cdd:cd14084   159 GLSkilgetSLMK--------------TLCGTPTYLAPEVLRSFGTEG--YTRAVDCWSLGVILFICLSGYPPFSEEY-- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 255 dcgwdrgevcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14084   221 ------------TQMSLKEQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
34-321 4.57e-63

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 202.18  E-value: 4.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYkLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14175     1 DGY-VVKETIGVGSYSVCKRCVHKATNMEYAVKVIDK----SKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC--ES--PEKvspVKICDFDLGSGMKLN 189
Cdd:cd14175    76 LMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdESgnPES---LRICDFGFAKQLRAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCtpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGWDRGEvcrvcqn 269
Cdd:cd14175   153 NGL-------LMTPCYTANFVAPEVL-----KRQGYDEGCDIWSLGILLYTMLAGYTPF-----ANGPSDTPE------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 KLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14175   209 EILTRIGSGKFTLSGGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
31-321 4.70e-62

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 201.02  E-value: 4.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYL 110
Cdd:cd14176    16 QFTDGYEVKEDI-GVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CESPEKvspVKICDFDLGSGM 186
Cdd:cd14176    91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyvdeSGNPES---IRICDFGFAKQL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 187 KLNNSCtpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcGADcgwDRGEvcrv 266
Cdd:cd14176   168 RAENGL-------LMTPCYTANFVAPEVL-----ERQGYDAACDIWSLGVLLYTMLTGYTPFAN--GPD---DTPE---- 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 267 cqnKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14176   227 ---EILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
33-321 1.28e-61

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 198.45  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEkqaghSRSRVFREVETLYQCQGNKNILELIEFFEDD------- 105
Cdd:cd14171     4 EEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILL-----DRPKARTEVRLHMMCSGHPNIVQIYDVYANSvqfpges 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 106 ---TRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDL 182
Cdd:cd14171    79 sprARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GsgmKLNNSctpittpELTTPCGSAEYMAPEVVE------------VFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14171   159 A---KVDQG-------DLMTPQFTPYYVAPQVLEaqrrhrkersgiPTSPTPYTYDKSCDMWSLGVIIYIMLCGYPPFYS 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 251 HCGAdcgwdrgevcRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14171   229 EHPS----------RTITKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
36-321 4.79e-61

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 196.89  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQN-GKEYAVKIIEK-------QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd14096     3 YRLINKI-GEGAFSNVYKAVPLRNtGKPVAIKVVRKadlssdnLKGSSRANILKEVQIMKRLS-HPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCES----------------PEK 171
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddETK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 172 VSP--------------VKICDFDLGSGMKLNNsctpittpeLTTPCGSAEYMAPEVVevfTDQatFYDKRCDLWSLGVV 237
Cdd:cd14096   161 VDEgefipgvggggigiVKLADFGLSKQVWDSN---------TKTPCGTVGYTAPEVV---KDE--RYSKKVDMWALGCV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 238 LYIMLSGYPPFvghcgadcgWDRGEvcrvcqNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd14096   227 LYTLLCGFPPF---------YDESI------ETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLA 291

                  ....
gi 1358101401 318 HPWV 321
Cdd:cd14096   292 HPWI 295
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
29-321 2.95e-60

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 194.11  E-value: 2.95e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  29 PGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDT 106
Cdd:cd14106     2 TENINEVYTVESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrRGQDCRNEILHEIAVLELCKDCPRVVNLHEVYETRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdlGSGM 186
Cdd:cd14106    82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDF--GISR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 187 KLNNSCtpittpELTTPCGSAEYMAPEVVEvftdqatfYDKRC---DLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEV 263
Cdd:cd14106   160 VIGEGE------EIREILGTPDYVAPEILS--------YEPISlatDMWSIGVLTYVLLTGHSPFGGD-------DKQET 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 264 crvcqnklFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14106   219 --------FLNISQCNLDFPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
39-320 6.25e-60

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 192.86  E-value: 6.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14185     4 IGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCE-SPEKVSPVKICDFDLGSgmklnnsctpITT 197
Cdd:cd14185    84 DLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhNPDKSTTLKLADFGLAK----------YVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGevcrvcQNKLFESIQE 277
Cdd:cd14185   154 GPIFTVCGTPTYVAPEIL-----SEKGYGLEVDMWAAGVILYILLCGFPPFRSP-------ERD------QEELFQIIQL 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 278 GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14185   216 GHYEFLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
34-320 2.12e-59

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 191.78  E-value: 2.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFR-EVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14184     1 EKYKI-GKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIEnEVSILRRVK-HPNIIMLIEEMDTPAELYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEKVSPVKICDFDLGsgmklnns 191
Cdd:cd14184    79 ELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvCEYPDGTKSLKLGDFGLA-------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 cTPITTPeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEvcRVCQNKL 271
Cdd:cd14184   151 -TVVEGP-LYTVCGTPTYVAPEII-----AETGYGLKVDIWAAGVITYILLCGFPPF-----------RSE--NNLQEDL 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 FESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14184   211 FDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
43-320 2.14e-59

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 191.33  E-value: 2.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGhSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDK-KKEAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGELLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPeKVSPVKICDFdlGSGMKLNNSCtpittpELTT 202
Cdd:cd14006    79 RLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR-PSPQIKIIDF--GLARKLNPGE------ELKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVE---VFTdqATfydkrcDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVCRvcqnklfeSIQEGK 279
Cdd:cd14006   150 IFGTPEFVAPEIVNgepVSL--AT------DMWSIGVLTYVLLSGLSPFLGE-------DDQETLA--------NISACR 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14006   207 VDFSEEYFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
31-326 1.44e-58

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 190.61  E-value: 1.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYL 110
Cdd:cd14177     1 QFTDVYEL-KEDIGVGSYSVCKRCIHRATNMEFAVKIIDK----SKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEKVSPVKICDFDLGSGMKLN 189
Cdd:cd14177    76 VTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFAKQLRGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCtpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGWDRGEvcrvcqn 269
Cdd:cd14177   156 NGL-------LLTPCYTANFVAPEVL-----MRQGYDAACDIWSLGVLLYTMLAGYTPF-----ANGPNDTPE------- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 270 KLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQ 326
Cdd:cd14177   212 EILLRIGSGKFSLSGGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQ 268
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-324 2.65e-57

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 187.34  E-value: 2.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGhsrSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14085     1 LEDFFEIESEL-GRGATSVVYRCRQKGTQKPYAVKKLKKTVD---KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgsgmklnns 191
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGL--------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 cTPITTPELT--TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEvcrvcqN 269
Cdd:cd14085   148 -SKIVDQQVTmkTVCGTPGYCAPEIL-----RGCAYGPEVDMWSVGVITYILLCGFEPFYD--------ERGD------Q 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 270 KLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd14085   208 YMFKRILNCDYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGK 262
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
41-323 2.82e-57

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 186.39  E-value: 2.82e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14167     9 EVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKeTSIENEIAVLHKIK-HPNIVALDDIYESGGHLYLIMQLVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgSGMKLNNSCtpittpe 199
Cdd:cd14167    88 LFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGL-SKIEGSGSV------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVcrvcqnKLFESIQEGK 279
Cdd:cd14167   160 MSTACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPF---------YDENDA------KLFEQILKAE 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd14167   220 YEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWIAG 263
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
41-320 9.63e-57

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 185.50  E-value: 9.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ------AGHSrsrVFREVETLYQCqGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiikekKVKY---VTIEKEVLSRL-AHPGIVKLYYTFQDESKLYFVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSpVKICDFdlGSGMKLNNSCTP 194
Cdd:cd05581    83 APNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD--EDMH-IKITDF--GTAKVLGPDSSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPE------------LTTPCGSAEYMAPEVVevfTDQATfyDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrge 262
Cdd:cd05581   158 ESTKGdadsqiaynqarAASFVGTAEYVSPELL---NEKPA--GKSSDLWALGCIIYQMLTGKPPFRG------------ 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 263 vcrVCQNKLFESIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL------SAAQVLQHPW 320
Cdd:cd05581   221 ---SNEYLTFQKIVKLEYEFPEN----FPPDAKDLIQKLLVLDPSKRLgvnengGYDELKAHPF 277
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
41-324 1.13e-56

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 185.09  E-value: 1.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14169     9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKeAMVENEIAVLRRIN-HENIVSLEDIYESPTHLYLAMELVTGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgSGMKLNNSctpittpe 199
Cdd:cd14169    88 LFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGL-SKIEAQGM-------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVEvftdQATfYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEvcrvcqNKLFESIQEGK 279
Cdd:cd14169   159 LSTACGTPGYVAPELLE----QKP-YGKAVDVWAIGVISYILLCGYPPF---------YDEND------SELFNQILKAE 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd14169   219 YEFDSPYWDDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGD 263
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
41-320 1.31e-56

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 184.29  E-value: 1.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA---GHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14099     7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSltkPKQREKLKSEIK-IHRSLKHPNIVKFHDCFEDEENVYILLELCSN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmklnnscTPITT 197
Cdd:cd14099    86 GSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKIGDFGLA---------ARLEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PEL--TTPCGSAEYMAPEVV--------EVftdqatfydkrcDLWSLGVVLYIMLSGYPPFvghcgaDCGwdrgevcrvC 267
Cdd:cd14099   154 DGErkKTLCGTPNYIAPEVLekkkghsfEV------------DIWSLGVILYTLLVGKPPF------ETS---------D 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 268 QNKLFESIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14099   207 VKETYKRIKKNEYSFPSHL--SISDEAKDLIRSMLQPDPTKRPSLDEILSHPF 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
40-320 2.16e-56

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 184.22  E-value: 2.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRSR--VFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14098     5 IDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRkvAGNDKNLqlFQREINIL-KSLEHPGIVRLIDWYEDDQHIYLVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpVKICDFDLGSgMKLNNSCtpi 195
Cdd:cd14098    84 EGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVI-VKISDFGLAK-VIHTGTF--- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 ttpeLTTPCGSAEYMAPEVV---EVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLF 272
Cdd:cd14098   159 ----LVTFCGTMAYLAPEILmskEQNLQGG--YSNLVDMWSVGCLVYVMLTGALPFDGS---------------SQLPVE 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 273 ESIQEGKY-EFPDKDWaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14098   218 KRIRKGRYtQPPLVDF-NISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
34-326 2.25e-56

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 185.24  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIekqagHSRSRVFREVETLYQCQGNKNILELIEFFEDDTR----FY 109
Cdd:cd14170     1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKML-----QDCPKARREVELHWRASQCPHIVRIVDVYENLYAgrkcLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQ--KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMK 187
Cdd:cd14170    76 IVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSctpittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrVC 267
Cdd:cd14170   156 SHNS--------LTTPCYTPYYVAPEVL-----GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL-----------AI 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 268 QNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQ 326
Cdd:cd14170   212 SPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTK 270
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
43-321 3.66e-56

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 183.52  E-value: 3.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKII-----EKQAGHSRSR---------VFREVETLYQCQgNKNILELIEFFEDDTR- 107
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlRKRREGKNDRgkiknalddVRREIAIMKKLD-HPNIVRLYEVIDDPESd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 -FYLVFEKLQGGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGS 184
Cdd:cd14008    80 kLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDF--GV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 185 GMKLNNSctpitTPELTTPCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevc 264
Cdd:cd14008   155 SEMFEDG-----NDTLQKTAGTPAFLAPELCDG--DSKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILE--------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 265 rvcqnkLFESIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14008   219 ------LYEAIQNQNDEFPIPP--ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
42-321 3.00e-55

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 180.81  E-value: 3.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIE-----KQAGHSRSRVFREVEtlyqcqgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14087     8 LIGRGSFSRVVRVEHRVTRQPYAIKMIEtkcrgREVCESELNVLRRVR-------HTNIIQLIEVFETKERVYMVMELAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTpit 196
Cdd:cd14087    81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGPNCL--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQ 276
Cdd:cd14087   158 ---MKTTCGTPEYIAPEIL-----LRKPYTQSVDMWAVGVIAYILLSGTMPFDDD---------------NRTRLYRQIL 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 277 EGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14087   215 RAKYSYSGEPWPSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
43-320 3.11e-55

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 180.50  E-value: 3.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLR-HPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 H-IQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPeKVSPVKICDFDLGSgmKLNnsctpiTTPELT 201
Cdd:cd14103    80 RvVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSR-TGNQIKIIDFGLAR--KYD------PDKKLK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 202 TPCGSAEYMAPEVVEVftDQATFydkRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvcqnklFESIQEGKYE 281
Cdd:cd14103   151 VLFGTPEFVAPEVVNY--EPISY---ATDMWSVGVICYVLLSGLSPFMGD-------NDAET--------LANVTRAKWD 210
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1358101401 282 FPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14103   211 FDDEAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPW 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
43-320 4.62e-55

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 180.11  E-value: 4.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQenLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKlnnsctpiTTPEL 200
Cdd:cd14009    80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQ--------PASMA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQN--KLFESIQEG 278
Cdd:cd14009   152 ETLCGSPLYMAPEIL-----QFQKYDAKADLWSVGAILFEMLVGKPPFRG-----------------SNhvQLLRNIERS 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 279 KYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14009   210 DAVIPFPIAAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
43-321 5.12e-55

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 180.46  E-value: 5.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQ--NGKEYAVKIIEKQAGhsrSRVF------REVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14080     8 IGEGSYSKVKLAEYTKsgLKEKVACKIIDKKKA---PKDFlekflpRELEILRKLR-HPNIIQVYSIFERGSKVFIFMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmKLnnsCTP 194
Cdd:cd14080    84 AEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSDFGFA---RL---CPD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPEL-TTPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVcrvcqNKLF 272
Cdd:cd14080   155 DDGDVLsKTFCGSAAYAAPEIL-----QGIPYDpKKYDIWSLGVILYIMLCGSMPF----------DDSNI-----KKML 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 273 ESIQEGKYEFPDKDWaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14080   215 KDQQNRKVRFPSSVK-KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
43-321 1.32e-54

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 178.99  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS---RVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14081     9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvlmKVEREI-AIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSgMKLNNSCtpittpe 199
Cdd:cd14081    88 LFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADFGMAS-LQPEGSL------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFvghcgaDCGWDRgevcrvcqnKLFESIQEG 278
Cdd:cd14081   157 LETSCGSPHYACPEVI-----KGEKYDgRKADIWSCGVILYALLVGALPF------DDDNLR---------QLLEKVKRG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14081   217 VFHIPH----FISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
Pkinase pfam00069
Protein kinase domain;
41-321 1.34e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.82  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-QAGHS-RSRVFREVETLYQCQGnKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKkDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDflhtkgiahrdlkpenilcespekvspvkicdfdlgsgmklnnsctpiTTP 198
Cdd:pfam00069  84 SLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------------------------------SGS 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcqNKLFESIQEG 278
Cdd:pfam00069 116 SLTTFVGTPWYMAPEVL-----GGNPYGPKVDVWSLGCILYELLTGKPPFPGING---------------NEIYELIIDQ 175
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDKdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:pfam00069 176 PYAFPEL-PSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
43-319 1.94e-54

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 177.46  E-value: 1.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-AGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEkLKKLLEELLREIEILKKLN-HPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTPITTPEL 200
Cdd:cd00180    80 DLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDSDDSLLKTTGGTT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TtpcgsAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLYIMlsgyppfvghcgadcgwdrgevcrvcqnklfesiqegky 280
Cdd:cd00180   157 P-----PYYAPPELLGG-----RYYGPKVDIWSLGVILYEL--------------------------------------- 187
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1358101401 281 efpdkdwahisSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd00180   188 -----------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
41-321 3.87e-54

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 178.10  E-value: 3.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVElSGDSEEELEALeREIRILSSLK-HPNIVRYLGTERTENTLNIFLEYVPGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFdlGSGMKLNNSCtpi 195
Cdd:cd06606    85 SLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL------VDSdgvVKLADF--GCAKRLAEIA--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGwDRGEVcrvcqnkLFESI 275
Cdd:cd06606   154 TGEGTKSLRGTPYWMAPEVI-----RGEGYGRAADIWSLGCTVIEMATGKPPW-----SELG-NPVAA-------LFKIG 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 276 QEGKY-EFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06606   216 SSGEPpPIPE----HLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
41-320 4.08e-54

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 178.63  E-value: 4.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE--------KQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14181    16 EVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnSC 192
Cdd:cd14181    96 DLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLH---IKLSDFGF--------SC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELTTPCGSAEYMAPEVVEVFTDQA-TFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVCrvcqnkL 271
Cdd:cd14181   165 HLEPGEKLRELCGTPGYLAPEILKCSMDEThPGYGKEVDLWACGVILFTLLAGSPPF---------WHRRQML------M 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 FESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14181   230 LRMIMEGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
36-317 4.24e-53

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 175.47  E-value: 4.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGH---SRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14014     2 YRLV-RLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEdeeFRERFLREARALARLS-HPNIVRVYDVGEDDGRPYIVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFDLGSGMkln 189
Cdd:cd14014    80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL------LTEdgrVKLTDFGIARAL--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nSCTPITTPelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEVcrvcQN 269
Cdd:cd14014   151 -GDSGLTQT--GSVLGTPAYMAPEQA-----RGGPVDPRSDIYSLGVVLYELLTGRPPF-----------DGDS----PA 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 270 KLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRL-SAAQVLQ 317
Cdd:cd14014   208 AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPqSAAELLA 256
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
29-324 8.42e-53

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 174.80  E-value: 8.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  29 PGKFEDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRF 108
Cdd:cd14183     1 PASISERYKV-GRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC-ESPEKVSPVKICDFDLGSgmk 187
Cdd:cd14183    80 YLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLAT--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 lnnsctpITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhCGADcgwdrgevcrvc 267
Cdd:cd14183   157 -------VVDGPLYTVCGTPTYVAPEII-----AETGYGLKVDIWAAGVITYILLCGFPPFRG-SGDD------------ 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 268 QNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd14183   212 QEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVNDD 268
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
41-321 1.42e-52

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 173.93  E-value: 1.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd05122     6 EKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCK-HPNIVKYYGSYLKKDELWIVMEFCSGGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSCTPITTpe 199
Cdd:cd05122    85 KDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE---VKLIDF--GLSAQLSDGKTRNTF-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 lttpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrGEVCRVcqnK-LFESIQEG 278
Cdd:cd05122   158 ----VGTPYWMAPEVI-----QGKPYGFKADIWSLGITAIEMAEGKPPY------------SELPPM---KaLFLIATNG 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDKDWAhiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd05122   214 PPGLRNPKKW--SKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
36-320 2.60e-52

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 173.36  E-value: 2.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-QAGHSR--SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14663     2 YEL-GRTLGEGTFAKVKFARNTKTGESVAIKIIDKeQVAREGmvEQIKREIAIMKLLR-HPNIVELHEVMATKTKIFFVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSgmkLNNSC 192
Cdd:cd14663    80 ELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN---LKISDFGLSA---LSEQF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTpeLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVcrvcqNKLF 272
Cdd:cd14663   154 RQDGL--LHTTCGTPNYVAPEVLA----RRGYDGAKADIWSCGVILFVLLAGYLPF----------DDENL-----MALY 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 273 ESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14663   213 RKIMKGEFEYP----RWFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
41-321 4.27e-52

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 172.57  E-value: 4.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA-GHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14078     9 ETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlGDDLPRVKTEIEALKNLS-HQHICRLYHVIETDNKIFMVLEYCPGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDL----GSGMKLNnsctpi 195
Cdd:cd14078    88 LFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN---LKLIDFGLcakpKGGMDHH------ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 ttpeLTTPCGSAEYMAPEVVevftdQATFY-DKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVcrvcqNKLFES 274
Cdd:cd14078   159 ----LETCCGSPAYAAPELI-----QGKPYiGSEADVWSMGVLLYALLCGFLPF----------DDDNV-----MALYRK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 275 IQEGKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14078   215 IQSGKYEEP--EW--LSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
43-321 6.57e-52

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 172.35  E-value: 6.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK-QAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14097     9 LGQGSFGVVIEATHKETQTKWAIKKINReKAGSSAVKLLeREVDILKHVN-HAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCES----PEKVSPVKICDFDLgSGMKLNNSctpit 196
Cdd:cd14097    88 KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidNNDKLNIKVTDFGL-SVQKYGLG----- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQ 276
Cdd:cd14097   162 EDMLQETCGTPIYMAPEVIS-----AHGYSQQCDIWSIGVIMYMLLCGEPPFVAK---------------SEEKLFEEIR 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 277 EGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14097   222 KGDLTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
31-321 1.23e-51

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 171.90  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQA------GHSRSRVFREVETLYQCQgNKNILELIEFFED 104
Cdd:cd14105     2 NVEDFYDIGEEL-GSGQFAVVKKCREKSTGLEYAAKFIKKRRskasrrGVSREDIEREVSILRQVL-HPNIITLHDVFEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPVKICDFDLG 183
Cdd:cd14105    80 KTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVPIPRIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMKLNNsctpittpELTTPCGSAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrg 261
Cdd:cd14105   160 HKIEDGN--------EFKNIFGTPEFVAPEIVnyEPLGLEA-------DMWSIGVITYILLSGASPFLGD---------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 262 evcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14105   215 -----TKQETLANITAVNYDFDDEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
41-323 1.79e-51

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 171.99  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGH--SRSRVFREVEtlyqcqgNKNILELIEFFEDDTRFYLV 111
Cdd:cd05580     7 KTLGTGSFGRVRLVKHKDSGKYYALKILKKakiiklkQVEHvlNEKRILSEVR-------HPFIVNLLGSFQDDRNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLnns 191
Cdd:cd05580    80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSD---GHIKITDF--GFAKRV--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpittPELT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGevcrvcQNK 270
Cdd:cd05580   152 ------KDRTyTLCGTPEYLAPEII-----LSKGHGKAVDWWALGILIYEMLAGYPPF---------FDEN------PMK 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 271 LFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05580   206 IYEKILEGKIRFP----SFFDPDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAG 259
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
32-322 2.43e-51

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 171.96  E-value: 2.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIE-----KQAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDT 106
Cdd:cd14094     1 FEDVYELC-EVIGKGPFSVVRRCIHRETGQQFAVKIVDvakftSSPGLSTEDLKREA-SICHMLKHPHIVELLETYSSDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSILAHIQKQKH----FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdl 182
Cdd:cd14094    79 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLnnsctPITTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrge 262
Cdd:cd14094   157 GVAIQL-----GESGLVAGGRVGTPHFMAPEVVK-----REPYGKPVDVWGCGVILFILLSGCLPFYG------------ 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 263 vcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14094   215 ----TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
41-324 3.41e-51

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 171.77  E-value: 3.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14168    16 EVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKeSSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLgSGMKLNNSCtpittpe 199
Cdd:cd14168    95 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGL-SKMEGKGDV------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEvcrvcqNKLFESIQEGK 279
Cdd:cd14168   167 MSTACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPF---------YDEND------SKLFEQILKAD 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd14168   227 YEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGD 271
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
41-322 8.80e-51

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 170.10  E-value: 8.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS---------RSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14182     9 EILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSfspeevqelREATLKEIDILRKVSGHPNIIQLKDTYETNTFFFLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnS 191
Cdd:cd14182    89 FDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN---IKLTDFGF--------S 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTPELTTPCGSAEYMAPEVVEV-FTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGevcrvcQNK 270
Cdd:cd14182   158 CQLDPGEKLREVCGTPGYLAPEIIECsMDDNHPGYGKEVDMWSTGVIMYTLLAGSPPF---------WHRK------QML 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 271 LFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14182   223 MLRMIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
46-323 1.89e-49

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 166.24  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  46 GAYAKVQGAVSLQNGKEYAVKIIEK---QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG---S 119
Cdd:cd05579     4 GAYGRVYLAKKKSTGDLYAIKVIKKrdmIRKNQVDSVLAERNILSQAQ-NPFVVKLYYSFQGKKNLYLVMEYLPGGdlyS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIqkqKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgSGMKLNNSCT------ 193
Cdd:cd05579    83 LLENV---GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH---LKLTDFGL-SKVGLVRRQIklsiqk 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 ---PITTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNK 270
Cdd:cd05579   156 ksnGAPEKEDRRIVGTPDYLAPEILL-----GQGHGKTVDWWSLGVILYEFLVGIPPFHAE---------------TPEE 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 271 LFESIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRL---SAAQVLQHPWVQG 323
Cdd:cd05579   216 IFQNILNGKIEWPEDP--EVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKG 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
31-321 1.08e-48

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 164.36  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQA------GHSRSRVFREVETLYQCQgNKNILELIEFFED 104
Cdd:cd14196     2 KVEDFYDIGEEL-GSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrGVSREEIEREVSILRQVL-HPNIITLHDVYEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPVKICDFDLG 183
Cdd:cd14196    80 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMKlnnsctpiTTPELTTPCGSAEYMAPEVVEvftdqatfYDK---RCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdr 260
Cdd:cd14196   160 HEIE--------DGVEFKNIFGTPEFVAPEIVN--------YEPlglEADMWSIGVITYILLSGASPFLGD--------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 261 gevcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14196   215 ------TKQETLANITAVSYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
36-317 1.97e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 169.04  E-value: 1.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:COG0515     9 YRIL-RLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADpeaRERFRREARALARLN-HPNIVRVYDVGEEDGRPYLVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGsgmklnnsc 192
Cdd:COG0515    87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL-TPDGR--VKLIDFGIA--------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELT---TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvcqn 269
Cdd:COG0515   155 RALGGATLTqtgTVVGTPGYMAPEQA-----RGEPVDPRSDVYSLGVTLYELLTGRPPFDGD-------SPAEL------ 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 270 klFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRL-SAAQVLQ 317
Cdd:COG0515   217 --LRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYqSAAELAA 263
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
36-320 1.30e-47

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 160.86  E-value: 1.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSeLLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS--RVFREVETLYQCQGNKNILELIEFFED--DTRFYLV 111
Cdd:cd05118     1 YEVLR-KIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAalREIKLLKHLNDVEGHPNIVKLLDVFEHrgGNHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEkLQGGSILAHIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFdlgsgmklnN 190
Cdd:cd05118    80 FE-LMGMNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ--LKLADF---------G 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCgadcgwdrgevcrvcqnk 270
Cdd:cd05118   148 LARSFTSPPYTPYVATRWYRAPEVLL----GAKPYGSSIDIWSLGCILAELLTGRPLFPGDS------------------ 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 271 lfesiqegkyefPDKDWAHI-----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd05118   206 ------------EVDQLAKIvrllgTPEALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
36-320 4.90e-47

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 159.36  E-value: 4.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA-GHSRS--RVFREVETLyQCQGNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14079     4 YIL-GKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKiKSLDMeeKIRREIQIL-KLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSc 192
Cdd:cd14079    82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN---VKIADFGLSNIMRDGEF- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 tpittpeLTTPCGSAEYMAPEVV--------EVftdqatfydkrcDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVc 264
Cdd:cd14079   158 -------LKTSCGSPNYAAPEVIsgklyagpEV------------DVWSCGVILYALLCGSLPF----------DDEHI- 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 265 rvcqNKLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14079   208 ----PNLFKKIKSGIYTIPS----HLSPGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
43-320 7.18e-47

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 159.18  E-value: 7.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGhsrSRVF------REVETLYQCQgNKNILELIEFFE-DDTRFYLVFEKL 115
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKA---PDDFvekflpRELEILARLN-HKSIIKTYEIFEtSDGKVYIVMELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLNNSCTPI 195
Cdd:cd14165    85 VQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKRCLRDENGRIV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTpelTTPCGSAEYMAPEVVevftdQATFYDKRC-DLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVcrvcqNKLFES 274
Cdd:cd14165   162 LS---KTFCGSAAYAAPEVL-----QGIPYDPRIyDIWSLGVILYIMVCGSMPY----------DDSNV-----KKMLKI 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 275 IQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14165   219 QKEHRVRFPRS--KNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
33-321 8.88e-47

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 159.41  E-value: 8.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQA------GHSRSRVFREVETLYQCQgNKNILELIEFFEDDT 106
Cdd:cd14194     4 DDYYDTGEEL-GSGQFAVVKKCREKSTGLQYAAKFIKKRRtkssrrGVSREDIEREVSILKEIQ-HPNVITLHEVYENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSP-VKICDFDLGSG 185
Cdd:cd14194    82 DVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPrIKIIDFGLAHK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 MKLNNsctpittpELTTPCGSAEYMAPEVVEvftdqatfYDK---RCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrge 262
Cdd:cd14194   162 IDFGN--------EFKNIFGTPEFVAPEIVN--------YEPlglEADMWSIGVITYILLSGASPFLGD----------- 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 263 vcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14194   215 ----TKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
35-321 1.26e-46

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 158.73  E-value: 1.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14074     4 LYDL-EETLGRGHFAVVKLARHVFTGEKVAVKVIDKTklDDVSKAHLFQEVRCMKLVQ-HPNVVRLYEVIDTQTKLYLIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSPVKICDFDLgsgmklNNS 191
Cdd:cd14074    82 ELGDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGF------SNK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITtpELTTPCGSAEYMAPEVVevftdQATFYDK-RCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgevcRVCQNK 270
Cdd:cd14074   154 FQPGE--KLETSCGSLAYSAPEIL-----LGDEYDApAVDIWSLGVILYMLVCGQPPFQ---------------EANDSE 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14074   212 TLTMIMDCKYTVPA----HVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
39-321 1.32e-46

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 158.54  E-value: 1.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14190     8 SKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLN-HRNLIQLYEAIETPNEIVLFMEYVEGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHI-QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLGSGMKLNNsctpitt 197
Cdd:cd14190    87 ELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTG-HQVKIIDFGLARRYNPRE------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pELTTPCGSAEYMAPEVVEVftDQATFydkRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvcqnklFESIQE 277
Cdd:cd14190   159 -KLKVNFGTPEFLSPEVVNY--DQVSF---PTDMWSMGVITYMLLSGLSPFLGD-------DDTET--------LNNVLM 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14190   218 GNWYFDEETFEHVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
34-321 1.50e-46

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 158.65  E-value: 1.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14088     1 DRYDL-GQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGsgmKLNNSCt 193
Cdd:cd14088    80 LATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLA---KLENGL- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pittpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcGWDRGEvcrvcqNKLFE 273
Cdd:cd14088   156 ------IKEPCGTPEYLAPEVV-----GRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEED-DYENHD------KNLFR 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14088   218 KILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
33-322 1.67e-46

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 158.63  E-value: 1.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQA------GHSRSRVFREVETLYQCQgNKNILELIEFFEDDT 106
Cdd:cd14195     4 EDHYEMGEEL-GSGQFAIVRKCREKGTGKEYAAKFIKKRRlsssrrGVSREEIEREVNILREIQ-HPNIITLHDIFENKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSP-VKICDFDLGSG 185
Cdd:cd14195    82 DVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPrIKLIDFGIAHK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 MKLNNsctpittpELTTPCGSAEYMAPEVVEvftdqatfYDK---RCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrge 262
Cdd:cd14195   162 IEAGN--------EFKNIFGTPEFVAPEIVN--------YEPlglEADMWSIGVITYILLSGASPFLGE----------- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 263 vcrvCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14195   215 ----TKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
41-321 1.37e-45

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 156.07  E-value: 1.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII------------EKQAGHSRS---RVFREVeTLYQCQGNKNILELIEFFEDD 105
Cdd:cd14077     7 KTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkerEKRLEKEISrdiRTIREA-ALSSLLNHPHICRLRDFLRTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 106 TRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDlgsg 185
Cdd:cd14077    86 NHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILI---SKSGNIKIIDFG---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 mkLNNSCTPITtpELTTPCGSAEYMAPEVVevftdQATFY-DKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVc 264
Cdd:cd14077   159 --LSNLYDPRR--LLRTFCGSLYFAAPELL-----QAQPYtGPEVDVWSFGVVLYVLVCGKVPF----------DDENM- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 265 rvcqNKLFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14077   219 ----PALHAKIKKGKVEYP----SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
43-319 2.40e-45

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 156.99  E-value: 2.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsRVFR--EVETLyqcQGNKNILELIE---F-------FEDDTRFYL 110
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLKKE------VIIEddDVECT---MTEKRVLALANrhpFltglhacFQTEDRLYF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDL-GSGMKLN 189
Cdd:cd05570    74 VMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAE---GHIKIADFGMcKEGIWGG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCtpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhCGADcgwdrgevcrvcqn 269
Cdd:cd05570   151 NTT--------STFCGTPDYIAPEIL-----REQDYGFSVDWWALGVLLYEMLAGQSPFEG-DDED-------------- 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 270 KLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHP 319
Cdd:cd05570   203 ELFEAILNDEVLYPR----WLSREAVSILKGLLTKDPARRLgcgpkGEADIKAHP 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
41-321 6.56e-45

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 154.08  E-value: 6.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK---QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14073     7 ETLGKGTYGKVKLAIERATGREVAIKSIKKdkiEDEQDMVRIRREIEIMSSLN-HPHIIRIYEVFENKDKIVIVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSctpitt 197
Cdd:cd14073    86 GELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGLSNLYSKDKL------ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 peLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQE 277
Cdd:cd14073   157 --LQTFCGSPLYASPEIVN----GTPYQGPEVDCWSLGVLLYTLVYGTMPFDGS---------------DFKRLVKQISS 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GKYEFPDKdwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14073   216 GDYREPTQ-----PSDASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
41-319 6.80e-45

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 154.16  E-value: 6.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII------EKQaghsRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd08215     6 RVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsnmsEKE----REEALNEVKLLSKLK-HPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK----HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlGSGMKLNN 190
Cdd:cd08215    81 ADGGDLAQKIKKQKkkgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFL-TKDGV--VKLGDF--GISKVLES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 sctpiTTPELTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNK 270
Cdd:cd08215   156 -----TTDLAKTVVGTPYYLSPELCE---NKP--YNYKSDIWALGCVLYELCTLKHPFEAN---------------NLPA 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 271 LFESIQEGKYE-FPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08215   211 LVYKIVKGQYPpIPS----QYSSELRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
32-321 1.50e-44

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 153.54  E-value: 1.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ--AGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFY 109
Cdd:cd14198     5 FNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRrrGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdlGSGMK 187
Cdd:cd14198    85 LILEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDF--GMSRK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSCtpittpELTTPCGSAEYMAPEVVEvftdqatfYD---KRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVc 264
Cdd:cd14198   163 IGHAC------ELREIMGTPEYLAPEILN--------YDpitTATDMWNIGVIAYMLLTHESPFVGE-------DNQET- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 265 rvcqnklFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14198   221 -------FLNISQVNVDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
43-321 2.23e-44

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 152.84  E-value: 2.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-AGHSRSRVF--REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14162     8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKkAPEDYLQKFlpREIEVIKGLK-HPNLICFYEAIETTSRVYIIMELAENGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSG-MKLNNSCTPITtp 198
Cdd:cd14162    87 LLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN---LKITDFGFARGvMKTKDGKPKLS-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elTTPCGSAEYMAPEVVEVFTDQATFydkrCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQN--KLFESIQ 276
Cdd:cd14162   162 --ETYCGSYAYASPEILRGIPYDPFL----SDIWSMGVVLYTMVYGRLPFDD-----------------SNlkVLLKQVQ 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 277 EgKYEFPDKdwAHISSEAKDLISKLLvRDAKQRLSAAQVLQHPWV 321
Cdd:cd14162   219 R-RVVFPKN--PTVSEECKDLILRML-SPVKKRITIEEIKRDPWF 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
40-322 4.51e-44

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 152.32  E-value: 4.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd14104     5 AEELGRGQFGIVHRCVETSSKKTYMAKFV-KVKGADQVLVKKEISILNIAR-HRNILRLHESFESHEELVMIFEFISGVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVSPVKICDF----DLGSGMKLNNSCTp 194
Cdd:cd14104    83 IFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCT-RRGSYIKIIEFgqsrQLKPGDKFRLQYT- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ittpelttpcgSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnkLFES 274
Cdd:cd14104   161 -----------SAEFYAPEVH-----QHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQ---------------TIEN 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 275 IQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14104   210 IRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWLK 257
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
42-320 6.18e-44

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 153.33  E-value: 6.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKV---QGAVSLQNGKEYAVKIIEKqaghsrSRVFREVETLYQCQGNKNILE---------LIEFFEDDTRFY 109
Cdd:cd05584     3 VLGKGGYGKVfqvRKTTGSDKGKIFAMKVLKK------ASIVRNQKDTAHTKAERNILEavkhpfivdLHYAFQTGGKLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLN 189
Cdd:cd05584    77 LILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQ---GHVKLTDFGLCKESIHD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadCGWDRgevcrvcqN 269
Cdd:cd05584   154 GTVT-------HTFCGTIEYMAPEIL-----TRSGHGKAVDWWSLGALMYDMLTGAPPF-------TAENR--------K 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 270 KLFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPW 320
Cdd:cd05584   207 KTIDKILKGKLNLP----PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPF 258
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
32-321 1.74e-43

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 150.86  E-value: 1.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLT-SELLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRF 108
Cdd:cd14197     5 FQERYSLSpGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKrrKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSgm 186
Cdd:cd14197    85 ILVLEYAAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSR-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 187 KLNNSctpittPELTTPCGSAEYMAPEVVEvftdqatfYDK---RCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEV 263
Cdd:cd14197   163 ILKNS------EELREIMGTPEYVAPEILS--------YEPistATDMWSIGVLAYVMLTGISPFLGD-------DKQET 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 264 crvcqnklFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14197   222 --------FLNISQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
41-321 1.81e-43

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 150.56  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE--KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14069     7 QTLGEGAFGEVFLAVNRNTEEAVAVKFVDmkRAPGDCPENIKKEVCIQKMLS-HKNVVRFYGHRREGEFQYLFLEYASGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNsctpiTTP 198
Cdd:cd14069    86 ELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN---LKISDFGLATVFRYKG-----KER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVvevfTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDrgEVCRVCQnkLFESIQEG 278
Cdd:cd14069   158 LLNKMCGTLPYVAPEL----LAKKKYRAEPVDVWSCGIVLFAMLAGELP----------WD--QPSDSCQ--EYSDWKEN 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 279 K--YEFPdkdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14069   220 KktYLTP---WKKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
42-321 1.94e-43

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 150.40  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVFREVETlyQCQ-GNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14186     8 LLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmvQRVRNEVEI--HCQlKHPSILELYNYFEDSNYVYLVLEMCHN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvKICDFDLGSGMKLNNSctpit 196
Cdd:cd14186    86 GEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNI---KIADFGLATQLKMPHE----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVcrvcQNKLfESIQ 276
Cdd:cd14186   158 --KHFTMCGTPNYISPEIA-----TRSAHGLESDVWSLGCMFYTLLVGRPPF----------DTDTV----KNTL-NKVV 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 277 EGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14186   216 LADYEMP----AFLSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
42-323 1.21e-42

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 150.90  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV--FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05573     8 VIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIahVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLN---------- 189
Cdd:cd05573    88 LMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL---DADGHIKLADFGLCTKMNKSgdresylnds 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 ------NSCTPITTPEL------TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadCG 257
Cdd:cd05573   165 vntlfqDNVLARRRPHKqrrvraYSAVGTPDYIAPEVL-----RGTGYGPECDWWSLGVILYEMLYGFPPF-------YS 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 258 WDRGEVC-RVCQNKlfESIQegkyeFPDKDwaHISSEAKDLISKLLvRDAKQRL-SAAQVLQHPWVQG 323
Cdd:cd05573   233 DSLVETYsKIMNWK--ESLV-----FPDDP--DVSPEAIDLIRRLL-CDPEDRLgSAEEIKAHPFFKG 290
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
41-320 1.23e-42

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 147.82  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEY-AVKIIEKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSLNKASTenLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEYCSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpVKICDFDLGSGMKLNNsctpitt 197
Cdd:cd14121    80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPV-LKLADFGFAQHLKPND------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnkLFESIQE 277
Cdd:cd14121   152 -EAHSLRGSPLYMAPEMI-----LKKKYDARVDLWSVGVILYECLFGRAPFASRSFEE---------------LEEKIRS 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GK-YEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14121   211 SKpIEIPTR--PELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
33-321 1.67e-42

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 147.84  E-value: 1.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14191     1 SDFYDI-EERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEI-SIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVSPVKICDFDLGSgmKLNNS 191
Cdd:cd14191    79 EMVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTKIKLIDFGLAR--RLENA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTpittpeLTTPCGSAEYMAPEVVEVftdQATFYDKrcDLWSLGVVLYIMLSGYPPFVGHCgadcgwdrgevcrvcQNKL 271
Cdd:cd14191   156 GS------LKVLFGTPEFVAPEVINY---EPIGYAT--DMWSIGVICYILVSGLSPFMGDN---------------DNET 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 FESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14191   210 LANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
34-321 2.16e-42

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 147.73  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKnILELIEFFEDDTRFYLVFE 113
Cdd:cd14114     2 DHYDILEEL-GTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPK-LINLHDAFEDDNEMVLILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVSPVKICDFDLGSgmKLN-NS 191
Cdd:cd14114    80 FLSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTT-KRSNEVKLIDFGLAT--HLDpKE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTpelttpcGSAEYMAPEVVEvfTDQATFYdkrCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVCRvcqnkl 271
Cdd:cd14114   157 SVKVTT-------GTAEFAAPEIVE--REPVGFY---TDMWAVGVLSYVLLSGLSPFAGE-------NDDETLR------ 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 feSIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14114   212 --NVKSCDWNFDDSAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
36-320 4.26e-42

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 147.48  E-value: 4.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd07832     2 YKILGRI-GEGAHGIVFKAKDRETGETVALKKValRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGG--SILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmKLNNS 191
Cdd:cd07832    81 YMLSSlsEVLRDEERP--LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV---LKIADFGLA---RLFSE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPittPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGE----VCRVC 267
Cdd:cd07832   153 EDP---RLYSHQVATRWYRAPELLY----GSRKYDEGVDLWAVGCIFAELLNGSPLFPGE-------NDIEqlaiVLRTL 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 268 QNKLFESIQE-------GKYEFPDKD---WAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07832   219 GTPNEKTWPEltslpdyNKITFPESKgirLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
36-321 4.50e-42

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 146.51  E-value: 4.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA--GHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14072     2 YRLL-KTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnPSSLQKLFREVRIM-KILNHPNIVKLFEVIETEKTLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDlgsgmkLNNSCT 193
Cdd:cd14072    80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDAD---MNIKIADFG------FSNEFT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITtpELTTPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQN--K 270
Cdd:cd14072   151 PGN--KLDTFCGSPPYAAPELF-----QGKKYDgPEVDVWSLGVILYTLVSGSLPFDG-----------------QNlkE 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14072   207 LRERVLRGKYRIP----FYMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
39-321 1.17e-41

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 145.83  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14193     8 KEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLN-HANLIQLYDAFESRNDIVLVMEYVDGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEkVSPVKICDFDLGSGMKlnnsctpiTT 197
Cdd:cd14193    87 ELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSRE-ANQVKIIDFGLARRYK--------PR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCgadcgwdrgevcrvcQNKLFESIQE 277
Cdd:cd14193   158 EKLRVNFGTPEFLAPEVVNY-----EFVSFPTDMWSLGVIAYMLLSGLSPFLGED---------------DNETLNNILA 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14193   218 CQWDFEDEEFADISEEAKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
43-321 3.96e-41

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 144.33  E-value: 3.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK----QAGhSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKVLFKaqleKAG-VEHQLRREVEIQSHLR-HPNILRLYGYFHDATRVYLILEYAPLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlgsGMKLNnscTPitTP 198
Cdd:cd14116    91 TVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGE---LKIADF----GWSVH---AP--SS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQEG 278
Cdd:cd14116   159 RRTTLCGTLDYLPPEMIE-----GRMHDEKVDLWSLGVLCYEFLVGKPPFEAN---------------TYQETYKRISRV 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14116   219 EFTFPD----FVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
43-323 4.15e-41

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 145.24  E-value: 4.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsrvfrEVETLYQCQ---GNKNILELIEF---------FEDDTRFYL 110
Cdd:cd14209     9 LGTGSFGRVMLVRHKETGNYYAMKILDKQ----------KVVKLKQVEhtlNEKRILQAINFpflvkleysFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSGMKLNN 190
Cdd:cd14209    79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQ---QGYIKVTDFGFAKRVKGRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SctpittpeltTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcRVCQnk 270
Cdd:cd14209   156 W----------TLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFFAD-------------QPIQ-- 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 271 LFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd14209   206 IYEKIVSGKVRFP----SHFSSDLKDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFAT 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
44-320 4.71e-41

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 143.94  E-value: 4.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  44 GEGAYAKVQGAVSLQNGKEYAVKIIEKQA---GHSRSRVFREVETLYQCQGNKnILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKcieKDSVRNVLNELEILQELEHPF-LVNLWYSFQDEEDMYMVVDLLLGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKvSPVKICDFdlgsgmklnNSCTPITTPEL 200
Cdd:cd05578    88 RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLD--EQ-GHVHITDF---------NIATKLTDGTL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTP-CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwDRGEVCRvcqnkLFESIQEgk 279
Cdd:cd05578   156 ATStSGTKPYMAPEVF-----MRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRT----SIEEIRA-----KFETASV-- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 280 yEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQ-VLQHPW 320
Cdd:cd05578   220 -LYP----AGWSEEAIDLINKLLERDPQKRLGDLSdLKNHPY 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
41-319 5.76e-41

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 143.51  E-value: 5.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVK--IIEKQaghSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd06614     6 EKIGEGASGEVYKATDRATGKEVAIKkmRLRKQ---NKELIINEILIMKECK-HPNIVDYYDSYLVGDELWVVMEYMDGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCTPIT 196
Cdd:cd06614    82 S-LTDIitQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKD---GSVKLADFGF---------AAQLT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 T--PELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqNKLFES 274
Cdd:cd06614   149 KekSKRNSVVGTPYWMAPEVI-----KRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPL--------------RALFLI 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 275 IQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd06614   210 TTKGIPPLKNPE--KWSPEFKDFLNKCLVKDPEKRPSAEELLQHP 252
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
41-321 1.39e-40

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 142.79  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLN-HVNLIQLYDAFESKTNLTLIMEYVDGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVSPVKICDFDLGSGMKlnnsctpiTTPE 199
Cdd:cd14192    89 FDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVN-STGNQIKIIDFGLARRYK--------PREK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdrgevcrvcqnklFESIQEGK 279
Cdd:cd14192   160 LKVNFGTPEFLAPEVVNY-----DFVSFPTDMWSVGVITYMLLSGLSPFLGETDAET---------------MNNIVNCK 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14192   220 WDFDAEAFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
34-321 1.80e-40

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 142.39  E-value: 1.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaGHSRSRVF---REVETLYQCQgNKNILELIEFFEDDTRFYL 110
Cdd:cd14002     1 ENYHVL-ELIGEGSFGKVYKGRRKYTGQVVALKFIPKR-GKSEKELRnlrQEIEILRKLN-HPNIIEMLDSFETKKEFVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGgSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvKICDFDLGSGMKLNn 190
Cdd:cd14002    78 VTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVV---KLCDFGFARAMSCN- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 sctpitTPELTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcrvCQNK 270
Cdd:cd14002   153 ------TLVLTSIKGTPLYMAPELVQ---EQP--YDHTADLWSLGCILYELFVGQPPF------------------YTNS 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 271 LFESIQEGKYE---FPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14002   204 IYQLVQMIVKDpvkWPSN----MSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
36-321 3.13e-40

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 141.71  E-value: 3.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLyQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14075     4 YRIRGEL-GSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQrlLSREISSM-EKLHHPNIIRLYEVVETLSKLHLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnSCT 193
Cdd:cd14075    82 YASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC---VKVGDFGF--------STH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPCGSAEYMAPevvEVFTDqATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEVCrvcqNKLFE 273
Cdd:cd14075   151 AKRGETLNTFCGSPPYAAP---ELFKD-EHYIGIYVDIWALGVLLYFMVTGVMPF-----------RAETV----AKLKK 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14075   212 CILEGTYTIPS----YVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
43-323 4.00e-40

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 141.76  E-value: 4.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV---QGAVSLQNGKEYAVKIIEKqaghsrSRVFREVETLYQCQGNKNILELIE---F-------FEDDTRFY 109
Cdd:cd05583     2 LGTGAYGKVflvRKVGGHDAGKLYAMKVLKK------ATIVQKAKTAEHTMTERQVLEAVRqspFlvtlhyaFQTDAKLH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMkln 189
Cdd:cd05583    76 LILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSE---GHVVLTDFGLSKEF--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nscTPITTPELTTPCGSAEYMAPEVVEVFTDQatfYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwDRGEvcRVCQN 269
Cdd:cd05583   150 ---LPGENDRAYSFCGTIEYMAPEVVRGGSDG---HDKAVDWWSLGVLTYELLTGASPFT---------VDGE--RNSQS 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 270 KLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05583   213 EISKRILKSHPPIPK----TFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFKG 267
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
41-323 5.92e-40

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 142.76  E-value: 5.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQgAVSLQN-GKEYAVKIIEKQAGHSRSRVFRevetlyqCQGNKNILELIE--F-------FEDDTRFYL 110
Cdd:cd05574     7 KLLGKGDVGRVY-LVRLKGtGKLFAMKVLDKEEMIKRNKVKR-------VLTEREILATLDhpFlptlyasFQTSTHLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQ--KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL---------------CESPEKVS 173
Cdd:cd05574    79 VMDYCPGGELFRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILlhesghimltdfdlsKQSSVTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 174 PVKICDFDLGSGMKLNNSCTPITTPELTTP----CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFV 249
Cdd:cd05574   159 PVRKSLRKGSRRSSVKSIEKETFVAEPSARsnsfVGTEEYIAPEVI-----KGDGHGSAVDWWTLGILLYEMLYGTTPFK 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 250 GHcgadcgwdrgevcrvCQNKLFESIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRL----SAAQVLQHPWVQG 323
Cdd:cd05574   234 GS---------------NRDETFSNILKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRG 294
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
41-320 5.93e-40

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 141.40  E-value: 5.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR--SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGg 118
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKqeSQLRNEVAILQQLS-HPGVVNLECMFETPERVFVVMEKLHG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSgmklnnsctpiT 196
Cdd:cd14082    87 DMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFAR-----------I 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPELT---TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrGEvcrvcQNKLFE 273
Cdd:cd14082   156 IGEKSfrrSVVGTPAYLAPEVL-----RNKGYNRSLDMWSVGVIIYVSLSGTFPF------------NE-----DEDIND 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 274 SIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14082   214 QIQNAAFMYPPNPWKEISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
43-320 6.61e-40

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 140.99  E-value: 6.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS--RVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14071     8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENlkKIYREVQIMKMLN-HPHIIKLYQVMETKDMLYLVTEYASNGEI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKlnnsctpiTTPEL 200
Cdd:cd14071    87 FDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDAN---MNIKIADFGFSNFFK--------PGELL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrVCQNkLFESIQEGKY 280
Cdd:cd14071   156 KTWCGSPPYAAPEVFE----GKEYEGPQLDIWSLGVVLYVLVCGALPFDGS--------------TLQT-LRDRVLSGRF 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1358101401 281 EFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14071   217 RIP----FFMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKW 252
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
41-323 7.19e-39

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 140.34  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsrvfrEVETLYQCQ---GNKNILE---------LIEFFEDDTRF 108
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKR----------EILKMKQVQhvaQEKSILMelshpfivnMMCSFQDENRV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKL 188
Cdd:PTZ00263   94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDF--GFAKKV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 nnsctpittPELT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVcrvc 267
Cdd:PTZ00263  169 ---------PDRTfTLCGTPEYLAPEVI-----QSKGHGKAVDWWTMGVLLYEFIAGYPPF---------FDDTPF---- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 268 qnKLFESIQEGKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSA-----AQVLQHPWVQG 323
Cdd:PTZ00263  222 --RIYEKILAGRLKFP--NW--FDGRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFHG 276
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
43-321 9.38e-39

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 137.77  E-value: 9.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQA----GHSRSRVFREVETLYQCQgNKNILELIEFFEDDT--RFYLVFEKLQ 116
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrriPNGEANVKREIQILRRLN-HRNVIKLVDVLYNEEkqKLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSI-LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvKICDFDLGSGMKLNNSCTPI 195
Cdd:cd14119    80 GGLQeMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTL---KISDFGVAEALDLFAEDDTC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPElttpcGSAEYMAPEVVevfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQN--KLFE 273
Cdd:cd14119   157 TTSQ-----GSPAFQPPEIA---NGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEG-----------------DNiyKLFE 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14119   212 NIGKGEYTIPD----DVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
43-321 1.18e-38

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 137.52  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS----RSRVFREV-------ETLyQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14004     8 MGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvRDRKLGTVpleihilDTL-NKRSHPNIVKLLDFFEDDEFYYLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKlQGGSI--LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsgmkln 189
Cdd:cd14004    87 MEK-HGSGMdlFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN---GTIKLIDF--------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevCRVcqn 269
Cdd:cd14004   154 GSAAYIKSGPFDTFVGTIDYAAPEVLR----GNPYGGKEQDIWALGVLLYTLVFKENPF---------------YNI--- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 klfESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14004   212 ---EEILEADLRIP----YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
41-321 1.47e-38

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 137.36  E-value: 1.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd06627     6 DLIGRGAFGSVYKGLNLNTGEFVAIKQIslEKIPKSDLKSVMGEIDLLKKLN-HPNIVKYIGSVKTKDSLYIILEYVENG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHIQKQ-KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlGSGMKLNNSctpitT 197
Cdd:cd06627    85 S-LASIIKKfGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILT---TKDGLVKLADF--GVATKLNEV-----E 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVEVftDQATFydkRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVcrvcqNKLFESIQE 277
Cdd:cd06627   154 KDENSVVGTPYWMAPEVIEM--SGVTT---ASDIWSVGCTVIELLTGNPPY---------YDLQPM-----AALFRIVQD 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06627   215 DHPPLPE----NISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
43-321 2.07e-38

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 137.62  E-value: 2.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-----QGAVSLQNGKEYAVKIIEK---QAGHSRSRVFREVETLYQCqGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14076     9 LGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRdtqQENCQTSKIMREINILKGL-THPNIVRLLDVLKTKKYIGIVLEF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLNNsctp 194
Cdd:cd14076    88 VSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLV---ITDFGFANTFDHFN---- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ittPEL-TTPCGSAEYMAPEVVevfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgaDCGWDRGEVCRVcqNKLFE 273
Cdd:cd14076   161 ---GDLmSTSCGSPCYAAPELV---VSDSMYAGRKADIWSCGVILYAMLAGYLPF------DDDPHNPNGDNV--PRLYR 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14076   227 YICNTPLIFPE----YVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
32-321 9.72e-38

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 135.33  E-value: 9.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIekqagHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14109     1 VRELYEIGEEDEKRAAQGAPFHVTERSTGRNFLAQLR-----YGDPFLMREVD-IHNSLDHPNIVQMHDAYDDEKLAVTV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGG----SILAHIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspekVSPVKICDFdlGSGMK 187
Cdd:cd14109    75 IDNLASTielvRDNLLPGKDY-YTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ----DDKLKLADF--GQSRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSctPITTPELttpcGSAEYMAPEVVEvfTDQATFYDkrcDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrVC 267
Cdd:cd14109   148 LLRG--KLTTLIY----GSPEFVSPEIVN--SYPVTLAT---DMWSVGVLTYVLLGGISPFLG---------------DN 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 268 QNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14109   202 DRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
39-320 1.47e-37

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 135.64  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKII---------EKQAGHSRSRVFREVETLYqcqgnknILELIEFFEDDTRFY 109
Cdd:cd05612     5 RIKTIGTGTFGRVHLVRDRISEHYYALKVMaipevirlkQEQHVHNEKRVLKEVSHPF-------IIRLFWTEHDQRFLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlGSGMKLN 189
Cdd:cd05612    78 MLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL---DKEGHIKLTDF--GFAKKLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NsctpittpELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQN 269
Cdd:cd05612   153 D--------RTWTLCGTPEYLAPEVI-----QSKGHNKAVDWWALGILIYEMLVGYPPFFDD---------------NPF 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 270 KLFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPW 320
Cdd:cd05612   205 GIYEKILAGKLEFP----RHLDLYAKDLIKKLLVVDRTRRLgnmknGADDVKNHRW 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
43-323 1.77e-37

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 134.66  E-value: 1.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGHsrsrVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKrhivqtrQQEH----IFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEYC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDF----DLGSGMKlnns 191
Cdd:cd05572    76 LGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS---NGYVKLVDFgfakKLGSGRK---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpittpelT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVCQNK 270
Cdd:cd05572   149 ---------TwTFCGTPEYVAPEII-----LNKGYDFSVDYWSLGILLYELLTGRPPFGG--------DDEDPMKIYNII 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 271 LFEsiqEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05572   207 LKG---IDKIEFPKY----IDKNAKNLIKQLLRRNPEERLgylkgGIRDIKKHKWFEG 257
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
43-312 1.77e-37

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 136.29  E-value: 1.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRnevKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDL-GSGMKLNNsctpiTTp 198
Cdd:cd05575    83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQ---GHVVLTDFGLcKEGIEPSD-----TT- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEvcrvcqnkLFESIQEG 278
Cdd:cd05575   154 --STFCGTPEYLAPEVLR---KQP--YDRTVDWWCLGAVLYEMLYGLPPFYSR-------DTAE--------MYDNILHK 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1358101401 279 KYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSA 312
Cdd:cd05575   212 PLRLRT----NVSPSARDLLEGLLQKDRTKRLGS 241
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
43-317 2.04e-37

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 134.20  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVslQNGKEYAVKIIEKQAGHSR-SRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd13999     1 IGSGSFGEVYKGK--WRGTDVAIKKLKVEDDNDElLKEFrREVSILSKLR-HPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmKLNNSctpiTTPE 199
Cdd:cd13999    78 YDLLHKKKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT---VKIADFGLS---RIKNS----TTEK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPevvEVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWdrgevcRVCQNKLFESIQEGk 279
Cdd:cd13999   148 MTGVVGTPRWMAP---EVLRGEP--YTEKADVYSFGIVLWELLTGEVPFKELSPIQIAA------AVVQKGLRPPIPPD- 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1358101401 280 yefpdkdwahISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd13999   216 ----------CPPELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
41-323 2.25e-37

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 136.20  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGHSRSRvfREVETLYQCQGnknILELIEFFEDDTRFYLVFE 113
Cdd:cd05599     7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKsemlekeQVAHVRAE--RDILAEADNPW---VVKLYYSFQDEENLYLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCT 193
Cdd:cd05599    82 FLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR---GHIKLSDFGL---------CT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELT-TPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadCGWDRGEVCRV---CQN 269
Cdd:cd05599   150 GLKKSHLAySTVGTPDYIAPEVFL-----QKGYGKECDWWSLGVIMYEMLIGYPPF-------CSDDPQETCRKimnWRE 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 270 KLfesiqegkyEFPDKdwAHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQG 323
Cdd:cd05599   218 TL---------VFPPE--VPISPEAKDLIERLLC-DAEHRLganGVEEIKSHPFFKG 262
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
43-323 3.05e-37

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 134.26  E-value: 3.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIekQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd06623     9 LGQGSSGVVYKVRHKPTGKIYALKKI--HVDGDeefRKQLLRELKTLRSCE-SPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEKVspvKICDF----DLGSGMKLNNsctp 194
Cdd:cd06623    86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEV---KIADFgiskVLENTLDQCN---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ittpeltTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVgHCGADCGWDRgeVCRVCQnklfes 274
Cdd:cd06623   159 -------TFVGTVTYMSPERI-----QGESYSYAADIWSLGLTLLECALGKFPFL-PPGQPSFFEL--MQAICD------ 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 275 iqEGKYEFPDKdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd06623   218 --GPPPSLPAE---EFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
63-320 3.09e-37

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 134.34  E-value: 3.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  63 YAVKIIEKqagHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDV 142
Cdd:cd14010    28 VAIKCVDK---SKRPEVLNEVRLTHELK-HPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 143 AAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDL-------------GSGMKLNNSCTPITTPELTTPCgsaeY 209
Cdd:cd14010   104 VRGLHYIHSKGIIYCDLKPSNILLDGN---GTLKLSDFGLarregeilkelfgQFSDEGNVNKVSKKQAKRGTPY----Y 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 210 MAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQEGKYEFP-DKDWA 288
Cdd:cd14010   177 MAPELF-----QGGVHSFASDLWALGCVLYEMFTGKPPFVAE---------------SFTELVEKILNEDPPPPpPKVSS 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1358101401 289 HISSEAKDLISKLLVRDAKQRLSAAQVLQHP-W 320
Cdd:cd14010   237 KPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
43-321 3.38e-37

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 134.41  E-value: 3.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK-----QAGHSR------------------SRVFREVETLYQCQgNKNILELI 99
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKkkllkQAGFFRrppprrkpgalgkpldplDRVYREIAILKKLD-HPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 100 EFFED--DTRFYLVFEKLQGGSILaHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKI 177
Cdd:cd14118    81 EVLDDpnEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH---VKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CDFDLGSGMKLNNSctpittpELTTPCGSAEYMAPEVVEvfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcg 257
Cdd:cd14118   157 ADFGVSNEFEGDDA-------LLSSTAGTPAFMAPEALS--ESRKKFSGKALDIWAMGVTLYCFVFGRCPFE-------- 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 258 wDRGEVCrvcqnkLFESIQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14118   220 -DDHILG------LHEKIKTDPVVFPDD--PVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
43-322 4.70e-37

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 133.84  E-value: 4.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKI-----IEKQAGHSRSRvfREVETlyQCQ-GNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVlfksqIEKEGVEHQLR--REIEI--QSHlRHPNILRLYNYFHDRKRIYLILEYAP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmklnnsctpIT 196
Cdd:cd14117    90 RGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE---LKIADFGWS-----------VH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPEL--TTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrVCQNKLFES 274
Cdd:cd14117   156 APSLrrRTMCGTLDYLPPEMIEGRT-----HDEKVDLWCIGVLCYELLVGMPPFES---------------ASHTETYRR 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 275 IQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14117   216 IVKVDLKFP----PFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
36-248 5.04e-37

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 133.63  E-value: 5.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEK-----QAGHSRSRVF--REVETLYQCQGNKNILELIEFFEDDTRF 108
Cdd:cd13993     2 YQLISPI-GEGAYGVVYLAVDLRTGRKYAIKCLYKsgpnsKDGNDFQKLPqlREIDLHRRVSRHPNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNERE--ASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFDLgsgm 186
Cdd:cd13993    81 YIVLEYCPNGDLFEAITENRIYVGKTelIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT--VKLCDFGL---- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 187 klnnSCTPITTPELTtpCGSAEYMAPEVV-EVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd13993   155 ----ATTEKISMDFG--VGSEFYMAPECFdEVGRSLKGYPCAAGDIWSLGIILLNLTFGRNPW 211
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
35-321 5.66e-37

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 133.13  E-value: 5.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFR------EVETLYQC--QGNKNILELIEFFEDDT 106
Cdd:cd14005     1 QYEVGDLL-GKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGpvpvplEIALLLKAskPGVPGVIRLLDWYERPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSIL-AHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSG 185
Cdd:cd14005    80 GFLLIMERPEPCQDLfDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINL--RTGEVKLIDF--GCG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 MKLNNSCtpittpeLTTPCGSAEYMAPEvvevFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgADCGWDRGEVcr 265
Cdd:cd14005   156 ALLKDSV-------YTDFDGTRVYSPPE----WIRHGRYHGRPATVWSLGILLYDMLCGDIPFE----NDEQILRGNV-- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 266 vcqnkLFesiqegkyefpdkdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14005   219 -----LF--------------RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
43-319 6.90e-37

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 132.88  E-value: 6.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-QGAVSLQNGKEYAVKIIEKQ-AGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14120     1 IGHGAFAVVfKGRHRKKPDLPVAIKCITKKnLSKSQNLLGKEIKILKELS-HENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSP------VKICDFdlGSGMKLNNSCTP 194
Cdd:cd14120    80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPspndirLKIADF--GFARFLQDGMMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTpelttpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdrgevcrvcqNKLFES 274
Cdd:cd14120   158 ATL------CGSPMYMAPEVI-----MSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQEL------------KAFYEK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 275 IQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14120   215 NANLRPNIP----SGTSPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
33-330 7.24e-37

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 133.71  E-value: 7.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd06611     4 NDIWEIIGEL-GDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECK-HPNIVGLYEAYFYENKLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNNs 191
Cdd:cd06611    82 EFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADF--GVSAKNKS- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpiTTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvgHCGADcgwdrgeVCRVcqnkL 271
Cdd:cd06611   156 ----TLQKRDTFIGTPYWMAPEVVACETFKDNPYDYKADIWSLGITLIELAQMEPP---HHELN-------PMRV----L 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 272 FEsIQEG---KYEFPDKdWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQgEQQHNGP 330
Cdd:cd06611   218 LK-ILKSeppTLDQPSK-W---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS-DQSDNKA 273
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
41-320 7.53e-37

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 134.79  E-value: 7.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVahtLTENRVLQNTR-HPFLTSLKYSFQTNDRLCFVMEYVNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDL-------GSGMKlnn 190
Cdd:cd05571    80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFGLckeeisyGATTK--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 sctpittpeltTPCGSAEYMAPEVVEVfTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgaDcgwdrgevcrvcQNK 270
Cdd:cd05571   154 -----------TFCGTPEYLAPEVLED-ND----YGRAVDWWGLGVVMYEMMCGRLPFYNR---D------------HEV 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 271 LFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPW 320
Cdd:cd05571   203 LFELILMEEVRFP----STLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPF 253
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
36-321 1.15e-36

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 133.15  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEK-----QAGHSR---------------------SRVFREVETLYQC 89
Cdd:cd14200     2 YKLQSEI-GKGSYGVVKLAYNESDDKYYAMKVLSKkkllkQYGFPRrppprgskaaqgeqakplaplERVYQEIAILKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  90 QgNKNILELIEFFED--DTRFYLVFEKLQGGSILaHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCE 167
Cdd:cd14200    81 D-HVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 168 SPekvSPVKICDFDLGSGMKLNNSctpittpELTTPCGSAEYMAPEVVEvfTDQATFYDKRCDLWSLGVVLYIMLSGYPP 247
Cdd:cd14200   159 DD---GHVKIADFGVSNQFEGNDA-------LLSSTAGTPAFMAPETLS--DSGQSFSGKALDVWAMGVTLYCFVYGKCP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 248 FVghcgadcgwdrGEVCRVCQNKlfesIQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14200   227 FI-----------DEFILALHNK----IKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
36-320 2.10e-36

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 132.40  E-value: 2.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRV--FREVETLYQCQGNKNILELIEFFEDDT--RFYLV 111
Cdd:cd07831     1 YKILGKI-GEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVnnLREIQALRRLSPHPNILRLIEVLFDRKtgRLALV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEkLQGGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespeKVSPVKICDFdlgsgmklnN 190
Cdd:cd07831    79 FE-LMDMNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI----KDDILKLADF---------G 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTPI-TTPELTTPCGSAEYMAPEVveVFTDqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRG 261
Cdd:cd07831   145 SCRGIySKPPYTEYISTRWYRAPEC--LLTD--GYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDqiakihdvLGTPDA 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 262 EVcrvcqNKLFESIQEGKYEFPDKD-------WAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07831   221 EV-----LKKFRKSRHMNYNFPSKKgtglrklLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
43-323 3.72e-36

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 132.89  E-value: 3.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsrVFRE---VE-TLYQCQ----GNKN--ILELIEFFEDDTRFYLVF 112
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKKD-------VVLEdddVEcTMIERRvlalASQHpfLTHLFCTFQTESHLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlgsGMKLNNSC 192
Cdd:cd05592    76 EYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADF----GMCKENIY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhCGADcgwdrgevcrvcqnKLF 272
Cdd:cd05592   149 GENKA---STFCGTPDYIAPEIL-----KGQKYNQSVDWWSFGVLLYEMLIGQSPFHG-EDED--------------ELF 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 273 ESIQEGKYEFPdkDWahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05592   206 WSICNDTPHYP--RW--LTKEAASCLSLLLERNPEKRLgvpecPAGDIRDHPFFKT 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
41-320 5.57e-36

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 130.78  E-value: 5.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCqGNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd14107     8 EEIGRGTFGFVKRVTHKGNGECCAAKFIPLRS-STRARAFQERDILARL-SHRRLTCLLDQFETRKTLILILELCSSEEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLgsgmklnnsCTPITTPEL 200
Cdd:cd14107    86 LDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTR-EDIKICDFGF---------AQEITPSEH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 T-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCgadcgwDRGEVCRVcqnklfesiQEGK 279
Cdd:cd14107   156 QfSKYGSPEFVAPEIV-----HQEPVSAATDIWALGVIAYLSLTCHSPFAGEN------DRATLLNV---------AEGV 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 280 YEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14107   216 VSWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
32-321 7.12e-36

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 130.48  E-value: 7.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 111
Cdd:cd14113     5 FDSFYSEVAEL-GRGRFSVVKKCDQRGTKRAVATKFVNKKL-MKRDQVTHELGVLQSLQ-HPQLVGLLDTFETPTSYILV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdlGSGMKLNns 191
Cdd:cd14113    82 LEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADF--GDAVQLN-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpiTTPELTTPCGSAEYMAPEVveVFTDQATFYDkrcDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgEVCRVCQNkl 271
Cdd:cd14113   158 ----TTYYIHQLLGSPEFAAPEI--ILGNPVSLTS---DLWSIGVLTYVLLSGVSPFLDE----------SVEETCLN-- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 fesIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14113   217 ---ICRLDFSFPDDYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
38-248 8.00e-36

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 130.32  E-value: 8.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVET---LYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14070     5 LIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRRegrIQQMIRHPNITQLLDILETENSYYLVMEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmklNNSCTP 194
Cdd:cd14070    85 CPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGLS-----NCAGIL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 195 ITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14070   157 GYSDPFSTQCGSPAYAAPELL-----ARKKYGPKVDVWSIGVNMYAMLTGTLPF 205
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
43-320 1.29e-35

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 129.70  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKM-KKKEQAAHEAALLQHLQ-HPQYITLHDTYESPTSYILVLELMDDGRLLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKIcdFDLGSGMKLNNSctpittPELTT 202
Cdd:cd14115    79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKL--IDLEDAVQISGH------RHVHH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDrgeVCRVcqnklfesiqegKYEF 282
Cdd:cd14115   151 LLGNPEFAAPEVI-----QGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCIN---VCRV------------DFSF 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1358101401 283 PDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14115   211 PDEYFGDVSQAARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
43-321 1.41e-35

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 129.73  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR------SRVFREVETLyqcqGNKNILELIEFFED-DTRFYLVFEKL 115
Cdd:cd14163     8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEfiqrflPRELQIVERL----DHKNIIHVYEMLESaDGKIYLVMELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEkvspVKICDFDLGSGMklnnsctPI 195
Cdd:cd14163    84 EDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQL-------PK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELT-TPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEVCR-VCQnklf 272
Cdd:cd14163   153 GGRELSqTFCGSTAYAAPEVL-----QGVPHDsRKGDIWSMGVVLYVMLCAQLPF----------DDTDIPKmLCQ---- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 273 esiQEGKYEFPdkdwAH--ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14163   214 ---QQKGVSLP----GHlgVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
42-321 1.77e-35

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 129.40  E-value: 1.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEkqAGHSRSRVFREVETLyQCQGN--KNIL--ELIEFF---EDDTRFYLVFEK 114
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVE--IDPINTEASKEVKAL-ECEIQllKNLQheRIVQYYgclQDEKSLSIFMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFdlGSGMKLNNSCTP 194
Cdd:cd06625    84 MPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDS---NGNVKLGDF--GASKRLQTICSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPELTtpcGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVCRVcqnkLFE- 273
Cdd:cd06625   159 TGMKSVT---GTPYWMSPEVINGEG-----YGRKADIWSVGCTVVEMLTTKPP----------WAEFEPMAA----IFKi 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06625   217 ATQPTNPQLPP----HVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
42-320 2.17e-35

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 130.77  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVthtLAERTVLAQVD-CPFIVPLKFSFQSPEKLYLVLAFINGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLgsgMKLNNSCTPITtp 198
Cdd:cd05585    80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIA---LCDFGL---CKLNMKDDDKT-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGevcrvcQNKLFESIQEG 278
Cdd:cd05585   152 --NTFCGTPEYLAPELL-----LGHGYTKAVDWWTLGVLLYEMLTGLPPF---------YDEN------TNEMYRKILQE 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 279 KYEFPDKdwahISSEAKDLISKLLVRDAKQRL---SAAQVLQHPW 320
Cdd:cd05585   210 PLRFPDG----FDRDAKDLLIGLLNRDPTKRLgynGAQEIKNHPF 250
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
36-320 3.39e-35

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 129.19  E-value: 3.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRV--FREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd07830     1 YKVIKQL-GDGTFGSVYLARNKETGELVAIKKM-KKKFYSWEECmnLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGgSILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKlnnS 191
Cdd:cd07830    79 YMEG-NLYQLMkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADFGLAREIR---S 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPittpeLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD-----C---------G 257
Cdd:cd07830   152 RPP-----YTDYVSTRWYRAPEILL----RSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDqlykiCsvlgtptkqD 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 258 WDRGEvcrvcqnKLFESIQegkYEFP-------DKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07830   223 WPEGY-------KLASKLG---FRFPqfaptslHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
43-320 5.78e-35

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 128.21  E-value: 5.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVfREVETLYQCQGNKNILELIE-FFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL-REYNISLELSVHPHIIKTYDvAFETEDYYVFAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEkVSPVKICDFDL----GSGMKLNNSCTPitt 197
Cdd:cd13987    80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKD-CRRVKLCDFGLtrrvGSTVKRVSGTIP--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pelttpcgsaeYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRgevcrvcqnklFESIQE 277
Cdd:cd13987   156 -----------YTAPEVCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEE-----------FVRWQK 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 278 GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQV---LQHPW 320
Cdd:cd13987   214 RKNTAVPSQWRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
44-321 6.79e-35

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 128.19  E-value: 6.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  44 GEGAYAKVQGAVSLQNGKEYAVKIIEKQagHSRSRVFREVetlyqcQGNKNILELI-----------EFFEDdtRFYLVF 112
Cdd:cd06626     9 GEGTFGKVYTAVNLDTGELMAMKEIRFQ--DNDPKTIKEI------ADEMKVLEGLdhpnlvryygvEVHRE--EVYIFM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNNSC 192
Cdd:cd06626    79 EYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSN---GLIKLGDF--GSAVKLKNNT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELTTPCGSAEYMAPevvEVFTDQATFYDKR-CDLWSLGVVLYIMLSGYPPfvghcgadcgWDRgevcrvCQNK- 270
Cdd:cd06626   154 TTMAPGEVNSLVGTPAYMAP---EVITGNKGEGHGRaADIWSLGCVVLEMATGKRP----------WSE------LDNEw 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 271 --LFESIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06626   215 aiMYHVGMGHKPPIPDSL--QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
41-322 8.02e-35

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 128.58  E-value: 8.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV---QGAVSLQNGKEYAVKIIEK--------QAGHSRSrvfrEVETLYQCQGNKNILELIEFFEDDTRFY 109
Cdd:cd05613     6 KVLGTGAYGKVflvRKVSGHDAGKLYAMKVLKKativqkakTAEHTRT----ERQVLEHIRQSPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLN 189
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVV---LTDFGLSKEFLLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NsctpitTPELTTPCGSAEYMAPEVVEvftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgADcgwdrGEvcRVCQN 269
Cdd:cd05613   159 E------NERAYSFCGTIEYMAPEIVR---GGDSGHDKAVDWWSLGVLMYELLTGASPFT----VD-----GE--KNSQA 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 270 KLFESIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQ 322
Cdd:cd05613   219 EISRRILKSEPPYPQE----MSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQ 272
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
41-323 1.46e-34

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 128.88  E-value: 1.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV---QGAVSLQNGKEYAVKIIEKQAghsrsrVFREVETLYQCQGNKNILELIE----------FFEDDTR 107
Cdd:cd05614     6 KVLGTGAYGKVflvRKVSGHDANKLYAMKVLRKAA------LVQKAKTVEHTRTERNVLEHVRqspflvtlhyAFQTDAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMk 187
Cdd:cd05614    80 LHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVV---LTDFGLSKEF- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 lnnsctpITTPELTTP--CGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwDRGEvcR 265
Cdd:cd05614   156 -------LTEEKERTYsfCGTIEYMAPEIIR----GKSGHGKAVDWWSLGILMFELLTGASPFT---------LEGE--K 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 266 VCQNKLFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAA-----QVLQHPWVQG 323
Cdd:cd05614   214 NTQSEVSRRILKCDPPFP----SFIGPVARDLLQKLLCKDPKKRLGAGpqgaqEIKEHPFFKG 272
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
42-319 1.79e-34

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 126.74  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd08530     7 KLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKERedSVNEIRLLASVN-HPNIIRYKEAFLDGNRLCIVMEYAPFGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKH----FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvKICDFDLGSGMKLNNSCTPI 195
Cdd:cd08530    86 LSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLV---KIGDLGISKVLKKNLAKTQI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPElttpcgsaeYMAPEVvevFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnkLFESI 275
Cdd:cd08530   163 GTPL---------YAAPEV---WKGRP--YDYKSDIWSLGCLLYEMATFRPPFEARTMQE---------------LRYKV 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 276 QEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08530   214 CRGKFPPIPPVY---SQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
46-320 1.83e-34

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 126.83  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  46 GAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV--FREVETLYQCQGNK-NILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd05611     7 GAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVtnVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLNGGDCAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLNNSCTPITtpeltt 202
Cdd:cd05611    87 LIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFGLSRNGLEKRHNKKFV------ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 pcGSAEYMAPEVVEVFTDqatfyDKRCDLWSLGVVLYIMLSGYPPFvgHCGAdcgwdrgevcrvcQNKLFESIQEGKYEF 282
Cdd:cd05611   158 --GTPDYLAPETILGVGD-----DKMSDWWSLGCVIFEFLFGYPPF--HAET-------------PDAVFDNILSRRINW 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 283 PDKDWAHISSEAKDLISKLLVRDAKQRLSA---AQVLQHPW 320
Cdd:cd05611   216 PEEVKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPF 256
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
41-321 2.12e-34

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 126.61  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd06612     9 EKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE--DLQEIIKEISILKQCD-SPYIVKYYGSYFKNTDLWIVMEYCGAGSV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQ-KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlGSGMKLNNsctpiTTPE 199
Cdd:cd06612    86 SDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL-NEEGQ--AKLADF--GVSGQLTD-----TMAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrGEV--CRVcqnkLFESIQE 277
Cdd:cd06612   156 RNTVIGTPFWMAPEVI-----QEIGYNNKADIWSLGITAIEMAEGKPPY------------SDIhpMRA----IFMIPNK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 278 GKYEFPD-KDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06612   215 PPPTLSDpEKW---SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
31-322 3.01e-34

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 126.28  E-value: 3.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKltsELLGEGAYAKV-QGAVSLQNGKEYAVKII-EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRF 108
Cdd:cd14202     1 KFEFSRK---DLIGHGAFAVVfKGRHKEKHDLEVAVKCInKKNLAKSQTLLGKEIKILKELK-HENIVALYDFQEIANSV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL--CESPEKVSP----VKICDFDL 182
Cdd:cd14202    77 YLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILlsYSGGRKSNPnnirIKIADFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLNNSCtpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdrge 262
Cdd:cd14202   157 ARYLQNNMMA--------ATLCGSPMYMAPEVI-----MSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL------ 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 263 vcrvcqNKLFESIQEGKYEFPDKDWAHIsseaKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14202   218 ------RLFYEKNKSLSPNIPRETSSHL----RQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
42-318 3.14e-34

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 126.20  E-value: 3.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ---AGHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14189     8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSrvaKPHQREKIVNEIE-LHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC-ESPEkvspVKICDFDLGSGMKlnnsctpit 196
Cdd:cd14189    87 S-LAHIWKARHtLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFInENME----LKVGDFGLAARLE--------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPEL--TTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgEVCRVcqNKLFES 274
Cdd:cd14189   153 PPEQrkKTICGTPNYLAPEVL---LRQG--HGPESDVWSLGCVMYTLLCGNPPF-------------ETLDL--KETYRC 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 275 IQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14189   213 IKQVKYTLP----ASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
41-318 5.39e-34

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 127.04  E-value: 5.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKN-ILELIEF-FEDDTRFYLVFEKLQGG 118
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHpFLTALKYaFQTHDRLCFVMEYANGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLgsgmklnnsCTPITTP 198
Cdd:cd05595    81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGL---------CKEGITD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELT--TPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgaDcgwdrgevcrvcQNKLFESIQ 276
Cdd:cd05595   149 GATmkTFCGTPEYLAPEVLE---DND--YGRAVDWWGLGVVMYEMMCGRLPFYNQ---D------------HERLFELIL 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 277 EGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQH 318
Cdd:cd05595   209 MEEIRFPRT----LSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEH 251
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
41-312 1.34e-33

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 126.24  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA---GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTilkKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLgsgmklnnsCTPITT 197
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVV---LTDFGL---------CKEGME 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTP--CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgEVCRVCQNKLFE-- 273
Cdd:cd05603   149 PEETTStfCGTPEYLAPEVL-----RKEPYDRTVDWWCLGAVLYEMLYGLPPFYSR----------DVSQMYDNILHKpl 213
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1358101401 274 SIQEGKyefpdkdwahiSSEAKDLISKLLVRDAKQRLSA 312
Cdd:cd05603   214 HLPGGK-----------TVAACDLLQGLLHKDQRRRLGA 241
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
41-321 2.03e-33

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 123.91  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSlQNGKEYAVKIIEK---QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14161     9 ETLGKGTYGRVKKARD-SSGRLVAIKSIRKdriKDEQDLLHIRREIEIMSSLN-HPHIISVYEVFENSSKIVIVMEYASR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKlnnsctpiTT 197
Cdd:cd14161    87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN---IKIADFGLSNLYN--------QD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVevftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQE 277
Cdd:cd14161   156 KFLQTYCGSPLYASPEIV----NGRPYIGPEVDSWSLGVLLYILVHGTMPFDGH---------------DYKILVKQISS 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 278 GKYEFPDKdwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14161   217 GAYREPTK-----PSDACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
41-321 5.34e-33

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 122.90  E-value: 5.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII-----EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVslvddDKKSRESVKQLEQEIALLSKLR-HPNIVQYYGTEREEDNLYIFLEYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlgsGMklnnsCTPI 195
Cdd:cd06632    85 PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADF----GM-----AKHV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTPC-GSAEYMAPEVVEvftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrGEVCRVCQNKLFES 274
Cdd:cd06632   153 EAFSFAKSFkGSPYWMAPEVIM---QKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGV------AAIFKIGNSGELPP 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 275 IqegkyefPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06632   224 I-------PD----HLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
41-321 6.99e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 122.74  E-value: 6.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQagHSRSRVF---REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd06609     7 ERIGKGSFGEVYKGIDKRTNQVVAIKVIDLE--EAEDEIEdiqQEIQFLSQCD-SPYITKYYGSFLKGSKLWIIMEYCGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFDLGSGMKLNNSctpit 196
Cdd:cd06609    84 GSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILlSEEGD----VKLADFGVSGQLTSTMS----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvgHCGADcgwdrgeVCRVcqnkLFESIQ 276
Cdd:cd06609   154 --KRNTFVGTPFWMAPEVI-----KQSGYDEKADIWSLGITAIELAKGEPP---LSDLH-------PMRV----LFLIPK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 277 egkyEFPDK-DWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06609   213 ----NNPPSlEGNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
41-323 7.78e-33

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 124.25  E-value: 7.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVectMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTPITT 197
Cdd:cd05590    81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHE---GHCKLADF----GMCKEGIFNGKTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQE 277
Cdd:cd05590   154 ---STFCGTPDYIAPEIL-----QEMLYGPSVDWWAMGVLLYEMLCGHAPFEAE---------------NEDDLFEAILN 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 278 GKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSA------AQVLQHPWVQG 323
Cdd:cd05590   211 DEVVYP--TW--LSQDAVDILKAFMTKNPTMRLGSltlggeEAILRHPFFKE 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
41-322 9.79e-33

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 122.58  E-value: 9.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQGN--KNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd06917     7 ELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvSDIQKEVALLSQLKLGqpKNIIKYYGSYLKGPSLWIIMDYCEG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNnsctpITT 197
Cdd:cd06917    87 GSIRTLMRAGP-IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLCDF--GVAASLN-----QNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcrvCQNKLFESIQE 277
Cdd:cd06917   156 SKRSTFVGTPYWMAPEVIT----EGKYYDTKADIWSLGITTYEMATGNPPY------------------SDVDALRAVML 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 278 -GKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06917   214 iPKSKPPRLEGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
43-321 1.28e-32

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 122.03  E-value: 1.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKE--YAVKIIEKQAGHSRSRVFREV---ETLYQCQ-GNKNILELIEFFEDDTRFY-LVFEKL 115
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGvlYAVKEYRRRDDESKRKDYVKRltsEYIISSKlHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlGSGMKLNNSCTPi 195
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL-DEDGV--LKLTDF--GTAEVFGMPAEK- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTPCGSAEYMAPEVVEvftdQATfYDKR-CDLWSLGVVLYIMLSGYPPFVGHCGADCGWdrgevcrvcqnKLFES 274
Cdd:cd13994   155 ESPMSAGLCGSEPYMAPEVFT----SGS-YDGRaVDVWSCGIVLFALFTGRFPWRSAKKSDSAY-----------KAYEK 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 275 IQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd13994   219 SGDFTNGPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
41-320 2.42e-32

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 121.82  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII---EKQAGHSRSRVfREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQg 117
Cdd:cd07829     5 EKLGEGTYGVVYKAKDKKTGEIVALKKIrldNEEEGIPSTAL-REISLLKELK-HPNIVKLLDVIHTENKLYLVFEYCD- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 gSILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFDLG--SGMKLNN 190
Cdd:cd07829    82 -QDLKKYldKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLL------INRdgvLKLADFGLAraFGIPLRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SctpitTPELTTPCgsaeYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcQ-N 269
Cdd:cd07829   155 Y-----THEVVTLW----YRAPEILL----GSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEID------------QlF 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 KLF-------ESIQEGKYEFPD----------KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07829   210 KIFqilgtptEESWPGVTKLPDykptfpkwpkNDLEKVlprlDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
36-321 3.66e-32

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 120.73  E-value: 3.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLtSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFE-DDTRFYLV 111
Cdd:cd14164     2 YTL-GTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPdfvQKFLPRELSILRRVN-HPNIVQMFECIEvANGRLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGgSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvsPVKICDFDLGSGMKlnns 191
Cdd:cd14164    80 MEAAAT-DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR--KIKIADFGFARFVE---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpiTTPEL-TTPCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEVCRVCQn 269
Cdd:cd14164   153 ----DYPELsTTFCGSRAYTPPEVI-----LGTPYDpKKYDVWSLGVVLYVMVTGTMPF-----------DETNVRRLR- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 klfesIQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14164   212 -----LQQRGVLYPSG--VALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
41-321 6.19e-32

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 120.07  E-value: 6.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEkqaghSRSRVFR----EVETL-----YQCQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14133     5 EVLGKGTFGQVVKCYDLLTGEEVALKIIK-----NNKDYLDqsldEIRLLellnkKDKADKYHIVRLKDVFYFKNHLCIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEkLQGGSILAHIQ--KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFdlGSgmkln 189
Cdd:cd14133    80 FE-LLSQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSR-CQIKIIDF--GS----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nSCTpiTTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcGADCGWDRGEVCRVCQN 269
Cdd:cd14133   151 -SCF--LTQRLYSYIQSRYYRAPEVI-----LGLPYDEKIDMWSLGCILAELYTGEPLFP---GASEVDQLARIIGTIGI 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 KLFESIQEGKYEFPDkdwahisseAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14133   220 PPAHMLDQGKADDEL---------FVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
34-322 9.65e-32

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 120.46  E-value: 9.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEK-----QAGHSR---------------------SRVFREVETLY 87
Cdd:cd14199     2 NQYKLKDEI-GKGSYGVVKLAYNEDDNTYYAMKVLSKkklmrQAGFPRrppprgaraapegctqprgpiERVYQEIAILK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  88 QCQgNKNILELIEFFED--DTRFYLVFEKLQGGSILaHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL 165
Cdd:cd14199    81 KLD-HPNVVKLVEVLDDpsEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 166 CESPekvSPVKICDFDLGSGMKLNNSCtpittpeLTTPCGSAEYMAPEVVEvfTDQATFYDKRCDLWSLGVVLYIMLSGY 245
Cdd:cd14199   159 VGED---GHIKIADFGVSNEFEGSDAL-------LTNTVGTPAFMAPETLS--ETRKIFSGKALDVWAMGVTLYCFVFGQ 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 246 PPFVghcgadcgwDRGEVCrvcqnkLFESIQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14199   227 CPFM---------DERILS------LHSKIKTQPLEFPDQ--PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
34-319 1.05e-31

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 119.77  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd06610     1 DDYELI-EVIGSGATAVVYAAYCLPKKEKVAIKRIDlEKCQTSMDELRKEIQAMSQCN-HPNVVSYYTSFVVGDELWLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILaHIQKQKH----FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFDLGSGMK 187
Cdd:cd06610    79 PLLSGGSLL-DIMKSSYprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILlGEDGS----VKIADFGVSASLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSCTPITTPELT-TPCgsaeYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgEVCRV 266
Cdd:cd06610   154 TGGDRTRKVRKTFVgTPC----WMAPEVME----QVRGYDFKADIWSFGITAIELATGAAPYSKYPPM-------KVLML 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 267 CQNKLFESIQEgkyefpDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd06610   219 TLQNDPPSLET------GADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
39-323 2.36e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 119.05  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS---RVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd05609     4 TIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNqiqQVFVERDILTFAE-NPFVVSMYCSFETKRHLCMVMEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLgSGMKLNNSCTPI 195
Cdd:cd05609    83 EGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITS---MGHIKLTDFGL-SKIGLMSLTTNL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 -------TTPELTTP--CGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEvcrv 266
Cdd:cd05609   159 yeghiekDTREFLDKqvCGTPEYIAPEVI---LRQG--YGKPVDWWAMGIILYEFLVGCVPFFG--------DTPE---- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 267 cqnKLFESIQEGKYEFPDKDWAhISSEAKDLISKLLVRDAKQRL---SAAQVLQHPWVQG 323
Cdd:cd05609   222 ---ELFGQVISDEIEWPEGDDA-LPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQD 277
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
42-319 2.49e-31

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 120.11  E-value: 2.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV-FREVETLYQCQGNKN-ILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05601     8 VIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsFFEEERDIMAKANSPwITKLQYAFQDSENLYLVMEYHPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFdlGSGMKLNNSCTpiTTP 198
Cdd:cd05601    88 LLSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILID---RTGHIKLADF--GSAAKLSSDKT--VTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELttPCGSAEYMAPEVVEVF-TDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrGEVCRVCQNKLfeSIQE 277
Cdd:cd05601   161 KM--PVGTPDYIAPEVLTSMnGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTE----------DTVIKTYSNIM--NFKK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 278 gKYEFPDKdwAHISSEAKDLISKLLVrDAKQRLSAAQVLQHP 319
Cdd:cd05601   227 -FLKFPED--PKVSESAVDLIKGLLT-DAKERLGYEGLCCHP 264
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
41-248 3.01e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 120.07  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR---VFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05604     2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEqkhIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSGMKLNNSCTpitt 197
Cdd:cd05604    82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDS---QGHIVLTDFGLCKEGISNSDTT---- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 198 pelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd05604   155 ---TTFCGTPEYLAPEVI-----RKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
36-318 4.91e-31

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 118.17  E-value: 4.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVEtLYQCQGNKNILELIEF----FEDDTRF-YL 110
Cdd:cd13986     2 YRIQ-RLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIE-NYRLFNHPNILRLLDSqivkEAGGKKEvYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQ----KQKHFNEREASRVVRDVAAALDFLH---TKGIAHRDLKPENILCESPEKvsPVKIcdfDLG 183
Cdd:cd13986    80 LLPYYKRGSLQDEIErrlvKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDE--PILM---DLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SG----MKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATfyDKRCDLWSLGVVLYIMLSGYPPFvghcgaDCGWD 259
Cdd:cd13986   155 SMnparIEIEGRREALALQDWAAEHCTMPYRAPELFDVKSHCTI--DEKTDIWSLGCTLYALMYGESPF------ERIFQ 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 260 RGEVCRVCqnklfesIQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd13986   227 KGDSLALA-------VLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
41-323 5.19e-31

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 119.80  E-value: 5.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVfreVETLYQCQGNKN-----ILELIEFFEDDTRFYLVFEKL 115
Cdd:cd05593    21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEV---AHTLTESRVLKNtrhpfLTSLKYSFQTKDRLCFVMEYV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLgsgmkLNNSCTPI 195
Cdd:cd05593    98 NGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGL-----CKEGITDA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTpeLTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESI 275
Cdd:cd05593   170 AT--MKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEKLFELI 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 276 QEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05593   228 LMEDIKFPRT----LSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFTG 276
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
31-328 5.54e-31

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 119.20  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKII--------EKQaghsrsRVFREVETLYQCQGNKNILELIEFF 102
Cdd:cd07852     8 RYEILKKL-----GKGAYGIVWKAIDKKTGEVVALKKIfdafrnatDAQ------RTFREIMFLQELNDHPNIIKLLNVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 --EDDTRFYLVFEKLQG-------GSILAHIQKQkhfnereasRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvs 173
Cdd:cd07852    77 raENDKDIYLVFEYMETdlhavirANILEDIHKQ---------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCR-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 174 pVKICDFDLG-SGMKLNNsctPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHC 252
Cdd:cd07852   146 -VKLADFGLArSLSQLEE---DDENPVLTDYVATRWYRAPEILL----GSTRYTKGVDMWSVGCILGEMLLGKPLFPGTS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 253 GAD--------CGWDRGEVCRVCQ----NKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07852   218 TLNqlekiievIGRPSAEDIESIQspfaATMLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPY 297

                  ....*...
gi 1358101401 321 VQgeQQHN 328
Cdd:cd07852   298 VA--QFHN 303
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
41-312 7.41e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 118.97  E-value: 7.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA---GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05602    13 KVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAilkKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYING 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLNNSCTpitt 197
Cdd:cd05602    93 GELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIV---LTDFGLCKENIEPNGTT---- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnkLFESIQE 277
Cdd:cd05602   166 ---STFCGTPEYLAPEVL-----HKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAE---------------MYDNILN 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1358101401 278 GKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSA 312
Cdd:cd05602   223 KPLQLK----PNITNSARHLLEGLLQKDRTKRLGA 253
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
30-322 7.90e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 117.42  E-value: 7.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYKltsELLGEGAYAKV-QGAVSLQNGKEYAVKIIEKQaGHSRSRVF--REVETLYQCQgNKNILELIEFFEDDT 106
Cdd:cd14201     4 GDFEYSRK---DLVGHGAFAVVfKGRHRKKTDWEVAIKSINKK-NLSKSQILlgKEIKILKELQ-HENIVALYDVQEMPN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEK----VSPVKICDFDL 182
Cdd:cd14201    79 SVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssVSGIRIKIADF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLNNSCTPITTpelttpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdrge 262
Cdd:cd14201   159 GFARYLQSNMMAATL------CGSPMYMAPEVI-----MSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL------ 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 263 vcrvcqNKLFESIQEGKYEFPDKDWAHISseakDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14201   222 ------RMFYEKNKNLQPSIPRETSPYLA----DLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
42-321 2.57e-30

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 116.09  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR---------VFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKdrkksmldaLQREIALLRELQ-HENIVQYLGSSSDANHLNIFL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSC 192
Cdd:cd06628    86 EYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG---IKISDFGISKKLEANSLS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITT--PELTtpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGWdrgevcrvcQNK 270
Cdd:cd06628   163 TKNNGarPSLQ---GSVFWMAPEVV-----KQTSYTRKADIWSLGCLVVEMLTGTHPF-----PDCTQ---------MQA 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06628   221 IFKIGENASPTIPS----NISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
42-310 4.78e-30

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 116.64  E-value: 4.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05616     7 VLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVectMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTPITTp 198
Cdd:cd05616    87 DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSE---GHIKIADF----GMCKENIWDGVTT- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQEG 278
Cdd:cd05616   159 --KTFCGTPDYIAPEIIAYQP-----YGKSVDWWAFGVLLYEMLAGQAPFEGE---------------DEDELFQSIMEH 216
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1358101401 279 KYEFPDKdwahISSEAKDLISKLLVRDAKQRL 310
Cdd:cd05616   217 NVAYPKS----MSKEAVAICKGLMTKHPGKRL 244
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
41-318 5.46e-30

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 114.72  E-value: 5.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK---QAGHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHsrvSKPHQREKIDKEIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSiLAHIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC-ESPEkvspVKICDFDLGSGMKlnnsctPI 195
Cdd:cd14188    86 RS-MAHILKaRKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFInENME----LKVGDFGLAARLE------PL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgEVCRVcqNKLFESI 275
Cdd:cd14188   155 EHRRRTI-CGTPNYLSPEVL-----NKQGHGCESDIWALGCVMYTMLLGRPPF-------------ETTNL--KETYRCI 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 276 QEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14188   214 REARYSLP----SSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
30-320 6.66e-30

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 115.49  E-value: 6.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEdmyklTSELLGEGAYAKVQGAVSLQNGKEYAVK--IIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd07833     1 NKYE-----VLGVVGEGAYGVVLKCRNKATGEIVAIKkfKESEDDEDVKKTALREVKVLRQLR-HENIVNLKEAFRRKGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLqGGSILAHIQKQKHFNEREASR-VVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFdlg 183
Cdd:cd07833    75 LYLVFEYV-ERTLLELLEASPGGLPPDAVRsYIWQLLQAIAYCHSHNIIHRDIKPENIL------VSEsgvLKLCDF--- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 sGMKLNNSCTPitTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGW----- 258
Cdd:cd07833   145 -GFARALTARP--ASPLTDYVATRWYRAPELLV----GDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYliqkc 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 259 ----DRGEVCRVCQNKLF-----------ESIQEgKYEfpdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07833   218 lgplPPSHQELFSSNPRFagvafpepsqpESLER-RYP------GKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
43-310 6.97e-30

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 115.95  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghsrsrVFRE-------VETLYQCQGNKN--ILELIEFFEDDTRFYLVFE 113
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKILKKDV------IIQDddvectmVEKRVLALSGKPpfLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCT 193
Cdd:cd05587    78 YVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAE---GHIKIADF----GMCKEGIFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEvcrvcqnkLFE 273
Cdd:cd05587   151 GKTT---RTFCGTPDYIAPEII-----AYQPYGKSVDWWAYGVLLYEMLAGQPPFDGE-------DEDE--------LFQ 207
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1358101401 274 SIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL 310
Cdd:cd05587   208 SIMEHNVSYPKS----LSKEAVSICKGLLTKHPAKRL 240
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
43-321 7.98e-30

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 114.46  E-value: 7.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSiLA 122
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HPNIVEMYSSYLVGDELWVVMEFLEGGA-LT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnsCTPIT--TPEL 200
Cdd:cd06648    93 DIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGR---VKLSDFGF---------CAQVSkeVPRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgevcrvcQNKLFESIQEGKY 280
Cdd:cd06648   161 KSLVGTPYWMAPEVISRLP-----YGTEVDIWSLGIMVIEMVDGEPPYF------------------NEPPLQAMKRIRD 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 281 EFPD--KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06648   218 NEPPklKNLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
41-319 9.36e-30

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 114.02  E-value: 9.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-AGHS-RSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPfRGPKeRARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQK---QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlgsGMklnnsCTPI 195
Cdd:cd13997    86 SLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI-SNKGT--CKIGDF----GL-----ATRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TT--PELTtpcGSAEYMAPEVVEVFtdqaTFYDKRCDLWSLGVVLYIMLSGYP-PFVGHcgadcGWdrgevcrvcqnklf 272
Cdd:cd13997   154 ETsgDVEE---GDSRYLAPELLNEN----YTHLPKADIFSLGVTVYEAATGEPlPRNGQ-----QW-------------- 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 273 ESIQEGKyeFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd13997   208 QQLRQGK--LPLPPGLVLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
43-320 1.29e-29

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 115.75  E-value: 1.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVetlyqcqGNKNILEL-----------IEF-FEDDTRFYL 110
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTI-------GERNILVRtaldespfivgLKFsFQTPTDLYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLNN 190
Cdd:cd05586    74 VTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIA---LCDFGLSKADLTDN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTpittpelTTPCGSAEYMAPEVVevfTDQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNK 270
Cdd:cd05586   151 KTT-------NTFCGTTEYLAPEVL---LDEKG-YTKMVDFWSLGVLVFEMCCGWSPFYAE---------------DTQQ 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 271 LFESIQEGKYEFPdKDwaHISSEAKDLISKLLVRDAKQRLSA----AQVLQHPW 320
Cdd:cd05586   205 MYRNIAFGKVRFP-KD--VLSDEGRSFVKGLLNRNPKHRLGAhddaVELKEHPF 255
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
33-321 1.31e-29

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 113.78  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELLgEGAYAKVQGAV--SLQNGKEYAVKIIEkqAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYL 110
Cdd:cd14112     2 TGRFSFGSEIF-RGRFSVIVKAVdsTTETDAHCAVKIFE--VSDEASEAVREFESLRTLQ-HENVQRLIAAFKPSNFAYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGgSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpVKICDFdlGSGMKLNN 190
Cdd:cd14112    78 VMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQ-VKLVDF--GRAQKVSK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTpittpelTTPCGSAEYMAPEVVEvfTDQATFydKRCDLWSLGVVLYIMLSGYPPFVGhcgadcGWDRGEVCRvcQNK 270
Cdd:cd14112   154 LGK-------VPVDGDTDWASPEFHN--PETPIT--VQSDIWGLGVLTFCLLSGFHPFTS------EYDDEEETK--ENV 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFEsiqegKYEfPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14112   215 IFV-----KCR-PNLIFVEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
43-323 1.62e-29

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 115.49  E-value: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGHsrsrVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd05598     9 IGVGAFGEVSLVRKKDTNALYAMKTLRKkdvlkrnQVAH----VKAERDILAEAD-NEWVVKLYYSFQDKENLYFVMDYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFDLGSGMKLNNSCTPI 195
Cdd:cd05598    84 PGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCTGFRWTHDSKYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTtpcGSAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvCQNKLfesI 275
Cdd:cd05598   161 LAHSLV---GTPNYIAPEVLLR-----TGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAE-----------TQLKV---I 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 276 QEGKY-EFPDKdwAHISSEAKDLISKLLvRDAKQRLS---AAQVLQHPWVQG 323
Cdd:cd05598   219 NWRTTlKIPHE--ANLSPEAKDLILRLC-CDAEDRLGrngADEIKAHPFFAG 267
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
41-322 1.69e-29

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 115.04  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVectMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlgsGMKLNNSctpITT 197
Cdd:cd05620    81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADF----GMCKENV---FGD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHcGADcgwdrgevcrvcQNKLFESIQE 277
Cdd:cd05620   151 NRASTFCGTPDYIAPEIL-----QGLKYTFSVDWWSFGVLLYEMLIGQSPF--H-GDD------------EDELFESIRV 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 278 GKYEFPdkDWahISSEAKDLISKLLVRDAKQRLS-AAQVLQHPWVQ 322
Cdd:cd05620   211 DTPHYP--RW--ITKESKDILEKLFERDPTRRLGvVGNIRGHPFFK 252
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
35-321 1.81e-29

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 113.55  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd06613     1 DYELIQRI-GSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECR-HPNIVAYFGSYLRRDKLWIVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFdlGSGMKLNNsct 193
Cdd:cd06613    79 CGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILlTEDGD----VKLADF--GVSAQLTA--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 piTTPELTTPCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPP-FVGHcgadcgwdrgeVCRVcqnkLF 272
Cdd:cd06613   150 --TIAKRKSFIGTPYWMAPEVAAV--ERKGGYDGKCDIWALGITAIELAELQPPmFDLH-----------PMRA----LF 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 273 esiQEGKYEFP-----DKD-WahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06613   211 ---LIPKSNFDppklkDKEkW---SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
42-317 2.67e-29

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 113.20  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELI--EFFEDDTR--FYLVFEkLQG 117
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLCGHPNIVQYYdsAILSSEGRkeVLLLME-YCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPEKvspVKICDFdlgsGMKLNNSCT 193
Cdd:cd13985    86 GSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR---FKLCDF----GSATTEHYP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPEL----------TTPcgsaEYMAPEVVEVFTDQATfyDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGEV 263
Cdd:cd13985   159 LERAEEVniieeeiqknTTP----MYRAPEMIDLYSKKPI--GEKADIWALGCLLYKLCFFKLPF----------DESSK 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 264 CRvcqnklfesIQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd13985   223 LA---------IVAGKYSIPEQP--RYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
42-320 3.54e-29

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 113.18  E-value: 3.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKI-------IEKQAGHSRSRVFREVEtLYQCQGNKNILELIEFFE-DDTRFYLVFE 113
Cdd:cd13990     7 LLGKGGFSEVYKAFDLVEQRYVACKIhqlnkdwSEEKKQNYIKHALREYE-IHKSLDHPRIVKLYDVFEiDTDSFCTVLE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK--GIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNS 191
Cdd:cd13990    86 YCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDDESY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctPITTPELTTP-CGSAEYMAPEVVEVfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvGHcgadcgwdrgevcRVCQNK 270
Cdd:cd13990   166 --NSDGMELTSQgAGTYWYLPPECFVV-GKTPPKISSKVDVWSVGVIFYQMLYGRKPF-GH-------------NQSQEA 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 271 LFES---IQEGKYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd13990   229 ILEEntiLKATEVEFPSK--PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
36-322 4.07e-29

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 114.16  E-value: 4.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSeLLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTR-----F 108
Cdd:cd07834     2 YELLK-PIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDDLIDAKRILREIKIL-RHLKHENIIGLLDILRPPSPeefndV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQggSILAHIQKQKHF-NEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLG 183
Cdd:cd07834    80 YIVTELME--TDLHKVIKSPQPlTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILvnsnCD-------LKICDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMklnnsCTPITTPELTtpcgsaEYM------APEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcg 257
Cdd:cd07834   151 RGV-----DPDEDKGFLT------EYVvtrwyrAPELLLSSKK----YTKAIDIWSVGCIFAELLTRKPLFPGRDYID-- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 258 wdrgevcrvcQ-NKLFESIQ-------------------EGKYEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAA 313
Cdd:cd07834   214 ----------QlNLIVEVLGtpseedlkfissekarnylKSLPKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITAD 283

                  ....*....
gi 1358101401 314 QVLQHPWVQ 322
Cdd:cd07834   284 EALAHPYLA 292
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
42-325 4.72e-29

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 114.40  E-value: 4.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV--FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05596    33 VIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSafFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 iLAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFdlGSGMKLN-----NSCTP 194
Cdd:cd05596   113 -LVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD---ASGHLKLADF--GTCMKMDkdglvRSDTA 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPElttpcgsaeYMAPEVVEVfTDQATFYDKRCDLWSLGVVLYIMLSGYPPF-----VG-------Hcgadcgwdrge 262
Cdd:cd05596   187 VGTPD---------YISPEVLKS-QGGDGVYGRECDWWSVGVFLYEMLVGDTPFyadslVGtygkimnH----------- 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 263 vcrvcQNKLfesiqegkyEFPDKDwaHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQGEQ 325
Cdd:cd05596   246 -----KNSL---------QFPDDV--EISKDAKSLICAFLT-DREVRLgrnGIEEIKAHPFFKNDQ 294
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
41-317 4.90e-29

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 112.77  E-value: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQgNKNIlelIEFF----EDDTrFYLVFEKL 115
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIRlTEKSSASEKVLREVKALAKLN-HPNI---VRYYtawvEEPP-LYIQMELC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHF---NEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFDLGSGMK----- 187
Cdd:cd13996    87 EGGTLRDWIDRRNSSsknDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIGDFGLATSIGnqkre 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 --LNNSCTPITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLsgYPPFVGHcgadcgwdrgEVCR 265
Cdd:cd13996   165 lnNLNNNNNGNTSNNSVGIGTPLYASPEQL-----DGENYNEKADIYSLGIILFEML--HPFKTAM----------ERST 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 266 VCQNKLfesiqegKYEFPDKDWAHISSEAkDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd13996   228 ILTDLR-------NGILPESFKAKHPKEA-DLIQSLLSKNPEERPSAEQLLR 271
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
41-323 4.91e-29

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 114.36  E-value: 4.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKN--ILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05594    31 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHpfLTALKYSFQTHDRLCFVMEYANGG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHT-KGIAHRDLKPENILCespEKVSPVKICDFDL-GSGMKLNNSctpit 196
Cdd:cd05594   111 ELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLML---DKDGHIKITDFGLcKEGIKDGAT----- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpeLTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQ 276
Cdd:cd05594   183 ---MKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---------------DHEKLFELIL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 277 EGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05594   240 MEEIRFPRT----LSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFAG 287
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
43-319 5.37e-29

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 113.65  E-value: 5.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV---QGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVEtlyqcqgnKNIL---------ELIEFFEDDTRFYL 110
Cdd:cd05582     3 LGQGSFGKVflvRKITGPDAGTLYAMKVLKKATLKVRDRVRTKME--------RDILadvnhpfivKLHYAFQTEGKLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnn 190
Cdd:cd05582    75 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDED---GHIKLTDFGL-------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTPITTPELT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEvcrvcqn 269
Cdd:cd05582   144 SKESIDHEKKAySFCGTVEYMAPEVV-----NRRGHTQSADWWSFGVLMFEMLTGSLPFQGK-------DRKE------- 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 270 kLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAA-----QVLQHP 319
Cdd:cd05582   205 -TMTMILKAKLGMPQ----FLSPEAQSLLRALFKRNPANRLGAGpdgveEIKRHP 254
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
41-322 8.57e-29

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 111.94  E-value: 8.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSi 120
Cdd:cd06647    13 EKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCTPItTPEL 200
Cdd:cd06647    91 LTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGF---------CAQI-TPEQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 ---TTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQNKL---FES 274
Cdd:cd06647   158 skrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMVEGEPPYLN-----------------ENPLralYLI 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 275 IQEGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06647   216 ATNGTPELQNPE--KLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
41-322 8.95e-29

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 113.48  E-value: 8.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05619    11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVectMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlgsGMKLNNSCTPITT 197
Cdd:cd05619    91 GDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHIKIADF----GMCKENMLGDAKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEvcrvcqnkLFESIQE 277
Cdd:cd05619   164 ---STFCGTPDYIAPEIL-----LGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQ-------DEEE--------LFQSIRM 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 278 GKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSA-AQVLQHPWVQ 322
Cdd:cd05619   221 DNPFYP--RW--LEKEAKDILVKLFVREPERRLGVrGDIRQHPFFR 262
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
42-314 9.31e-29

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 113.55  E-value: 9.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05615    17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVectMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTPITTP 198
Cdd:cd05615    97 DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSE---GHIKIADF----GMCKEHMVEGVTTR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELttpCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQEG 278
Cdd:cd05615   170 TF---CGTPDYIAPEIIAYQP-----YGRSVDWWAYGVLLYEMLAGQPPFDGE---------------DEDELFQSIMEH 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1358101401 279 KYEFPDKdwahISSEAKDLISKLLVRDAKQRLSAAQ 314
Cdd:cd05615   227 NVSYPKS----LSKEAVSICKGLMTKHPAKRLGCGP 258
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
41-323 1.09e-28

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 113.21  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVqGAVSLQN-GKEYAVKIIEKQAGHSRSRV--FREvETLYQCQGNKN-ILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05597     7 KVIGRGAFGEV-AVVKLKStEKVYAMKILNKWEMLKRAETacFRE-ERDVLVNGDRRwITKLHYAFQDENYLYLVMDYYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKqkhFNEREASRVVRDVAA----ALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFdlGSGMKLNNSC 192
Cdd:cd05597    85 GGDLLTLLSK---FEDRLPEEMARFYLAemvlAIDSIHQLGYVHRDIKPDNVLLD---RNGHIRLADF--GSCLKLREDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTPELTTPcgsaEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRVCQNKlf 272
Cdd:cd05597   157 TVQSSVAVGTP----DYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVE------TYGKIMNHK-- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 273 esiqeGKYEFPDkDWAHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQG 323
Cdd:cd05597   225 -----EHFSFPD-DEDDVSEEAKDLIRRLIC-SRERRLgqnGIDDFKKHPFFEG 271
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
33-319 1.09e-28

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 112.21  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKiiekqaghsrsRVF-------REVETLYQCQgNKNILELIEFF--- 102
Cdd:cd14137     3 EISYTIE-KVIGSGSFGVVYQAKLLETGEVVAIK-----------KVLqdkryknRELQIMRRLK-HPNIVKLKYFFyss 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 ---EDDTRFYLVFEKLQGgSILAHIQKQKHFNEREASRVVR----DVAAALDFLHTKGIAHRDLKPENILCeSPEKVSpV 175
Cdd:cd14137    70 gekKDEVYLNLVMEYMPE-TLYRVIRHYSKNKQTIPIIYVKlysyQLFRGLAYLHSLGICHRDIKPQNLLV-DPETGV-L 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 176 KICDFdlGSGMKLNNSctpittpELTTP--CgSAEYMAPEVveVFtdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCG 253
Cdd:cd14137   147 KLCDF--GSAKRLVPG-------EPNVSyiC-SRYYRAPEL--IF--GATDYTTAIDIWSAGCVLAELLLGQPLFPGESS 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 254 ADcgwDRGEVCRVcqnkL----FESIQE-----GKYEFPD---KDW-----AHISSEAKDLISKLLVRDAKQRLSAAQVL 316
Cdd:cd14137   213 VD---QLVEIIKV----LgtptREQIKAmnpnyTEFKFPQikpHPWekvfpKRTPPDAIDLLSKILVYNPSKRLTALEAL 285

                  ...
gi 1358101401 317 QHP 319
Cdd:cd14137   286 AHP 288
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
43-318 1.42e-28

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 111.21  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVsLQNGKEYAVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAASKKEFlTELEMLGRLR-HPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKhfNEREAS-----RVVRDVAAALDFLHTKG---IAHRDLKPENILC-ESPEkvsPvKICDFDLGSGMKLNNSc 192
Cdd:cd14066    79 DRLHCHK--GSPPLPwpqrlKIAKGIARGLEYLHEECpppIIHGDIKSSNILLdEDFE---P-KLTDFGLARLIPPSES- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 tpitTPELTTPCGSAEYMAPEVVEvfTDQATfydKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLF 272
Cdd:cd14066   152 ----VSKTSAVKGTIGYLAPEYIR--TGRVS---TKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVESKGKEEL 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 273 ESIQEgkyEFPDKDWAHISSEAKDLISKLLV---RDAKQRLSAAQVLQH 318
Cdd:cd14066   223 EDILD---KRLVDDDGVEEEEVEALLRLALLctrSDPSLRPSMKEVVQM 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
41-319 2.89e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 110.32  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--------EKQAGHSRSRVFREVEtlyqcqgNKNILELIEFFED--DTRFYL 110
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDGKILVWKEIdygkmsekEKQQLVSEVNILRELK-------HPNIVRYYDRIVDraNTTLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNER--EAS--RVVRDVAAALDFLHTKG-----IAHRDLKPENI-LCESPEkvspVKICDF 180
Cdd:cd08217    79 VMEYCEGGDLAQLIKKCKKENQYipEEFiwKIFTQLLLALYECHNRSvgggkILHRDLKPANIfLDSDNN----VKLGDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 DLGSGMKLNNSCTpittpelTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdr 260
Cdd:cd08217   155 GLARVLSHDSSFA-------KTYVGTPYYMSPELLN---EQS--YDEKSDIWSLGCLIYELCALHPPFQAA--------- 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 261 gevcrvCQNKLFESIQEGKYEF-PDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08217   214 ------NQLELAKKIKEGKFPRiPS----RYSSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
33-321 1.55e-27

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 108.96  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd06643     4 EDFWEIVGEL-GDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCD-HPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILA-HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNS 191
Cdd:cd06643    82 EFCAGGAVDAvMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD---GDIKLADF----GVSAKNT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgwdRGEVcrvcqNKL 271
Cdd:cd06643   155 ---RTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQIEPP------------HHEL-----NPM 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 272 FESIQEGKYEFPD----KDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06643   215 RVLLKIAKSEPPTlaqpSRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
29-321 1.72e-27

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 108.54  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  29 PGKFEDMykltsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHsRSRVFREVETLYQCQGNKNILELIEFF------ 102
Cdd:cd06608     5 AGIFELV-----EVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDE-EEEIKLEINILRKFSNHPNIATFYGAFikkdpp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 EDDTRFYLVFEKLQGGSILAHIQKQKHFNER--EA--SRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKI 177
Cdd:cd06608    79 GGDDQLWLVMEYCGGGSVTDLVKGLRKKGKRlkEEwiAYILRETLRGLAYLHENKVIHRDIKGQNILlTEEAE----VKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CDFDLGSGMKLN----NSCTpittpelTTPCgsaeYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcg 253
Cdd:cd06608   155 VDFGVSAQLDSTlgrrNTFI-------GTPY----WMAPEVIACDQQPDASYDARCDVWSLGITAIELADGKPPL----- 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 254 ADCGWDRGevcrvcqnkLFEsIQEGKYE--FPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06608   219 CDMHPMRA---------LFK-IPRNPPPtlKSPEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
43-320 4.07e-27

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 109.74  E-value: 4.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVfREVETlyqcqgNKNIL---------ELIEFFEDDTRFYLVFE 113
Cdd:cd05600    19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEV-NHVLT------ERDILtttnspwlvKLLYAFQDPENVYLAME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSG-------- 185
Cdd:cd05600    92 YVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDS---SGHIKLTDFGLASGtlspkkie 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 ---MKLNNSCTPITTpELT--------------------TPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIML 242
Cdd:cd05600   169 smkIRLEEVKNTAFL-ELTakerrniyramrkedqnyanSVVGSPDYMAPEVLR---GEG--YDLTVDYWSLGCILFECL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 243 SGYPPFvghCGADCgwdrgevcrvcqNKLFESI-------QEGKYEFPDKDWAhISSEAKDLISKLLVrDAKQRL-SAAQ 314
Cdd:cd05600   243 VGFPPF---SGSTP------------NETWANLyhwkktlQRPVYTDPDLEFN-LSDEAWDLITKLIT-DPQDRLqSPEQ 305

                  ....*.
gi 1358101401 315 VLQHPW 320
Cdd:cd05600   306 IKNHPF 311
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
40-330 4.16e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 109.14  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SEL-----LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS-RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:PLN00034   74 SELervnrIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTvRRQICREIEILRDVN-HPNVVKCHDMFDHNGEIQVLLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSIL-AHIQKqkhfnEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSC 192
Cdd:PLN00034  153 FMDGGSLEgTHIAD-----EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADF--GVSRILAQTM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPIttpelTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGV-VLYIMLSGYPPFVGHCGadcGWdRGEVCRVCqnkl 271
Cdd:PLN00034  223 DPC-----NSSVGTIAYMSPERINTDLNHGAYDGYAGDIWSLGVsILEFYLGRFPFGVGRQG---DW-ASLMCAIC---- 289
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 fesiqegkYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQHNGP 330
Cdd:PLN00034  290 --------MSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQ 340
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
39-323 5.61e-27

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 109.17  E-value: 5.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKqaghsrSRVFREvETLYQCQGNKNIL---------ELIEFFEDDTRFY 109
Cdd:cd05629     5 TVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLK------SEMFKK-DQLAHVKAERDVLaesdspwvvSLYYSFQDAQYLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFDLGSG---- 185
Cdd:cd05629    78 LIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID---RGGHIKLSDFGLSTGfhkq 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 ------MKL--NNSCTP---------ITTPELT-------------------TPCGSAEYMAPEVvevFTDQAtfYDKRC 229
Cdd:cd05629   155 hdsayyQKLlqGKSNKNridnrnsvaVDSINLTmsskdqiatwkknrrlmaySTVGTPDYIAPEI---FLQQG--YGQEC 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 230 DLWSLGVVLYIMLSGYPPFvghcgadCGWDRGEVCRVCQNkLFESIQegkyeFPDKdwAHISSEAKDLISKLLVrDAKQR 309
Cdd:cd05629   230 DWWSLGAIMFECLIGWPPF-------CSENSHETYRKIIN-WRETLY-----FPDD--IHLSVEAEDLIRRLIT-NAENR 293
                         330
                  ....*....|....*..
gi 1358101401 310 L---SAAQVLQHPWVQG 323
Cdd:cd05629   294 LgrgGAHEIKSHPFFRG 310
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
34-322 7.94e-27

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 107.04  E-value: 7.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd06644    12 EVWEIIGEL-GDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCN-HPYIVKLLGAFYWDGKLWIMIE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILA-HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSc 192
Cdd:cd06644    90 FCPGGAVDAiMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD---GDIKLADF----GVSAKNV- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 tpITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgwdRGEVcrvcqNKLF 272
Cdd:cd06644   162 --KTLQRRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPP------------HHEL-----NPMR 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 273 ESIQEGKYEFPDKD----WahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06644   223 VLLKIAKSEPPTLSqpskW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
41-323 1.02e-26

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 108.22  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGHSRSrvfrEVETLYQCQGnKNILELIEFFEDDTRFYLVFE 113
Cdd:cd05627     8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKadmlekeQVAHIRA----ERDILVEADG-AWVVKMFYSFQDKRNLYLIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMK------ 187
Cdd:cd05627    83 FLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLKkahrte 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 -----LNNSCTPITTPELTTP-----------------CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGY 245
Cdd:cd05627   160 fyrnlTHNPPSDFSFQNMNSKrkaetwkknrrqlaystVGTPDYIAPEVF-----MQTGYNKLCDWWSLGVIMYEMLIGY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 246 PPFvghcgadCGWDRGEVCRVCQNklfesiQEGKYEFPDKdwAHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQ 322
Cdd:cd05627   235 PPF-------CSETPQETYRKVMN------WKETLVFPPE--VPISEKAKDLILRFCT-DAENRIgsnGVEEIKSHPFFE 298

                  .
gi 1358101401 323 G 323
Cdd:cd05627   299 G 299
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
41-321 1.04e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 106.31  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE---KQAGHSRSR-------VFREVETLYQCQgNKNILELIEFFEDDTRFYL 110
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVElpkTSSDRADSRqktvvdaLKSEIDTLKDLD-HPNIVQYLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL------CespekvspvKICDFdlGS 184
Cdd:cd06629    86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILvdlegiC---------KISDF--GI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 185 GMKLNNSctpITTPELTTPCGSAEYMAPEVVEvftDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVC 264
Cdd:cd06629   155 SKKSDDI---YGNNGATSMQGSVFWMAPEVIH---SQGQGYSAKVDIWSLGCVVLEMLAGRRP----------WSDDEAI 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 265 RVcqnkLFESIQEgKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06629   219 AA----MFKLGNK-RSAPPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
41-320 1.10e-26

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 107.58  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVdctMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTPITT 197
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE---GHCKLADF----GMCKEGILNGKTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcGADcgwdrgevcrvCQNKLFESIQE 277
Cdd:cd05591   154 ---TTFCGTPDYIAPEIL-----QELEYGPSVDWWALGVLMYEMMAGQPPF----EAD-----------NEDDLFESILH 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 278 GKYEFPdkDWahISSEAKDLISKLLVRDAKQRLSA-------AQVLQHPW 320
Cdd:cd05591   211 DDVLYP--VW--LSKEAVSILKAFMTKNPAKRLGCvasqggeDAIRQHPF 256
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
34-320 1.28e-26

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 105.75  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd14108     2 DYYDIHKEI-GRGAFSYLRRVKEKSSDLSFAAKFIPVRA-KKKTSARRELALLAELD-HKSIVRFHDAFEKRRVVIIVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 kLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSPVKICDFdlGSGMKLnnsct 193
Cdd:cd14108    79 -LCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLM-ADQKTDQVRICDF--GNAQEL----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pitTPELTTPC--GSAEYMAPEVVevftDQATFyDKRCDLWSLGVVLYIMLSGYPPFVGHCgadcgwDRGEVCrvcqnkl 271
Cdd:cd14108   150 ---TPNEPQYCkyGTPEFVAPEIV----NQSPV-SKVTDIWPVGVIAYLCLTGISPFVGEN------DRTTLM------- 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 272 feSIQEGKYEFPDKDWAHISSEAKDLISKLLVRDaKQRLSAAQVLQHPW 320
Cdd:cd14108   209 --NIRNYNVAFEESMFKDLCREAKGFIIKVLVSD-RLRPDAEETLEHPW 254
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
43-322 1.59e-26

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 105.89  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS-RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEAlQKQILRELDVLHKCN-SPYIVGFYGAFYSEGDISICMEYMDGGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEKvspVKICDFDLgSGmKLNNSCTpittpel 200
Cdd:cd06605    88 KILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ---VKLCDFGV-SG-QLVDSLA------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSG---YPPfvghcgadcgWDRGEVCRVCQnkLFESI-Q 276
Cdd:cd06605   156 KTFVGTRSYMAPERI-----SGGKYTVKSDIWSLGLSLVELATGrfpYPP----------PNAKPSMMIFE--LLSYIvD 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 277 EGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06605   219 EPPPLLPSGKF---SPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
41-325 1.78e-26

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 107.78  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05621    58 KVIGRGAFGEVQLVRHKASQKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlGSGMKLNNSctpiTTP 198
Cdd:cd05621   138 D-LVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADF--GTCMKMDET----GMV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVEVFTDQAtFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrGEVCRVCQNKlfesiqeG 278
Cdd:cd05621   208 HCDTAVGTPDYISPEVLKSQGGDG-YYGRECDWWSVGVFLFEMLVGDTPFYADSLV------GTYSKIMDHK-------N 273
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 279 KYEFPDKdwAHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQGEQ 325
Cdd:cd05621   274 SLNFPDD--VEISKHAKNLICAFLT-DREVRLgrnGVEEIKQHPFFRNDQ 320
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
43-312 1.83e-26

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 107.00  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSrvfrEVETLYqCQgnKNILELIE-----F-------FEDDTRFYL 110
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARD----EVESLM-CE--KRIFETVNsarhpFlvnlfacFQTPEHVCF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQkQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDL---GSGMK 187
Cdd:cd05589    80 VMEYAAGGDLMMHIH-EDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLckeGMGFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSctpittpeltTPCGSAEYMAPEVVevfTDqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvc 267
Cdd:cd05589   156 DRTS----------TFCGTPEFLAPEVL---TD--TSYTRAVDWWGLGVLIYEMLVGESPFPGD-------DEEEV---- 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 268 qnklFESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSA 312
Cdd:cd05589   210 ----FDSIVNDEVRYP----RFLSTEAISIMRRLLRKNPERRLGA 246
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
33-315 2.14e-26

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 107.82  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLtsELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-------QAGHSRSR--VFREVETLYqcqgnknILELIEFFE 103
Cdd:cd05628     1 EDFESL--KVIGRGAFGEVRLVQKKDTGHVYAMKILRKadmlekeQVGHIRAErdILVEADSLW-------VVKMFYSFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLG 183
Cdd:cd05628    72 DKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMK----------LNNSC-TPITTPELTTP-----------------CGSAEYMAPEVVevftdQATFYDKRCDLWSLG 235
Cdd:cd05628   149 TGLKkahrtefyrnLNHSLpSDFTFQNMNSKrkaetwkrnrrqlafstVGTPDYIAPEVF-----MQTGYNKLCDWWSLG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 236 VVLYIMLSGYPPFvghcgadcgwdrgevCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVrDAKQRLSAAQV 315
Cdd:cd05628   224 VIMYEMLIGYPPF---------------CSETPQETYKKVMNWKETLIFPPEVPISEKAKDLILRFCC-EWEHRIGAPGV 287
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
41-331 3.58e-26

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 106.22  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLyQCQGNKNILELIEFF------EDDTRFYLVF 112
Cdd:cd07851    21 SPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfQSAIHAKRTYRELRLL-KHMKHENVIGLLDVFtpasslEDFQDVYLVT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLqgGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGsgmKL 188
Cdd:cd07851   100 HLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAvnedCE-------LKILDFGLA---RH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNSctpittpELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDR 260
Cdd:cd07851   168 TDD-------EMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGKTLFPGSDHIDqlkrimnlVGTPD 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 261 GEVCRVCQNKLFESIQEGKYEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPWVqgEQQHNGPD 331
Cdd:cd07851   237 EELLKKISSESARNYIQSLPQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYL--AEYHDPED 309
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
41-319 3.68e-26

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 104.31  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII-EKQAG-HSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEkLQGG 118
Cdd:cd14050     7 SKLGEGSFGEVFKVRSREDGKLYAVKRSrSRFRGeKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTE-LCDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKLNNSCTPITtp 198
Cdd:cd14050    86 SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL-SKDGV--CKLGDFGLVVELDKEDIHDAQE-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elttpcGSAEYMAPEVVE-VFTdqatfydKRCDLWSLGVVL-----YIMLSGYPPfvghcgadcGWdrgevcrvcqnklf 272
Cdd:cd14050   161 ------GDPRYMAPELLQgSFT-------KAADIFSLGITIlelacNLELPSGGD---------GW-------------- 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 273 ESIQEGkyEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14050   205 HQLRQG--YLPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
42-310 3.90e-26

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 106.64  E-value: 3.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR---VFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05617    22 VIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDidwVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMklnnsCTPITTP 198
Cdd:cd05617   102 DLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD---GHIKLTDY----GM-----CKEGLGP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTP--CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgaDCGWDRGEVCrvCQNKLFESIQ 276
Cdd:cd05617   170 GDTTStfCGTPNYIAPEIL-----RGEEYGFSVDWWALGVLMFEMMAGRSPF------DIITDNPDMN--TEDYLFQVIL 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1358101401 277 EGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRL 310
Cdd:cd05617   237 EKPIRIP----RFLSVKASHVLKGFLNKDPKERL 266
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
41-325 4.29e-26

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 107.40  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05622    79 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfeMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlGSGMKLNNSctpiTTP 198
Cdd:cd05622   159 D-LVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADF--GTCMKMNKE----GMV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPEVVEVFTDQAtFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrGEVCRVCQNKlfesiqeG 278
Cdd:cd05622   229 RCDTAVGTPDYISPEVLKSQGGDG-YYGRECDWWSVGVFLYEMLVGDTPFYADSLV------GTYSKIMNHK-------N 294
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 279 KYEFPDKdwAHISSEAKDLISKLLVrDAKQRL---SAAQVLQHPWVQGEQ 325
Cdd:cd05622   295 SLTFPDD--NDISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLFFKNDQ 341
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
81-320 4.62e-26

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 103.97  E-value: 4.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  81 REVETLYQCQGNKNILELIEFFEDDTRFYLVFEKlQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLK 160
Cdd:cd14023    33 DKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEK-DFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 161 PENILCESPEKvSPVKICDFDLGSGMKLNNSCtpittpeLTTPCGSAEYMAPEVVEVftdQATFYDKRCDLWSLGVVLYI 240
Cdd:cd14023   112 LRKFVFSDEER-TQLRLESLEDTHIMKGEDDA-------LSDKHGCPAYVSPEILNT---TGTYSGKSADVWSLGVMLYT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 241 MLSGYPPFvgHcGADcgwdrgevcrvcQNKLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14023   181 LLVGRYPF--H-DSD------------PSALFSKIRRGQFCIPD----HVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
36-320 6.89e-26

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 103.84  E-value: 6.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELLGEGAYAKVQGAVSLQNGKEYA---VKIiEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd13983     2 YLKFNEVLGRGSFKTVYRAFDTEEGIEVAwneIKL-RKLPKAERQRFKQEIEILKSLK-HPNIIKFYDSWESKSKKEVIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 --EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPEKVspVKICDFDLGSGMKL 188
Cdd:cd13983    80 itELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGE--VKIGDLGLATLLRQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNSCTPITTPElttpcgsaeYMAPEVVEvftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgEvcrvCQ 268
Cdd:cd13983   158 SFAKSVIGTPE---------FMAPEMYE------EHYDEKVDIYAFGMCLLEMATGEYPYS------------E----CT 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 269 N--KLFESIQEGKyeFPDKDWAHISSEAKDLISKLLvRDAKQRLSAAQVLQHPW 320
Cdd:cd13983   207 NaaQIYKKVTSGI--KPESLSKVKDPELKDFIEKCL-KPPDERPSARELLEHPF 257
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
41-318 9.89e-26

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 103.99  E-value: 9.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVqgaVSLQN---GKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14046    12 QVLGKGAFGQV---VKVRNkldGRYYAIKKIKLRSESKNnSRILREVMLLSRLN-HQHVVRYYQAWIERANLYIQMEYCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLN------- 189
Cdd:cd14046    88 KSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGLATSNKLNvelatqd 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 -NSCTPITTPE---LTTPCGSAEYMAPEVVEVFTDQatfYDKRCDLWSLGVVLYIMLsgYPPFVGHcgadcgwDRGEVCR 265
Cdd:cd14046   165 iNKSTSAALGSsgdLTGNVGTALYVAPEVQSGTKST---YNEKVDMYSLGIIFFEMC--YPFSTGM-------ERVQILT 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 266 vcqnklfeSIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14046   233 --------ALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
41-322 1.01e-25

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 104.42  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSi 120
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCTPItTPEL 200
Cdd:cd06656   103 LTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGF---------CAQI-TPEQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 ---TTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqNKLFESIQE 277
Cdd:cd06656   170 skrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMVEGEPPYLNENPL--------------RALYLIATN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 278 GKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06656   231 GTPELQNPE--RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
41-319 1.12e-25

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 103.45  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSlQNGKEYAVKIIEKQaGHSRSRV---FREVETLYQCQGNKNILELI--EFFEDDTRFYLVFEKl 115
Cdd:cd14131     7 KQLGKGGSSKVYKVLN-PKKKIYALKRVDLE-GADEQTLqsyKNEIELLKKLKGSDRIIQLYdyEVTDEDDYLYMVMEC- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 qGGSILAHIQKQKH---FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespekVS-PVKICDFdlGSGMKLNNS 191
Cdd:cd14131    84 -GEIDLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-----VKgRLKLIDF--GIAKAIQND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTpelTTPCGSAEYMAPEVVeVFTDQATFYDKR------CDLWSLGVVLYIMLSGYPPFvGHCgadcgwdrgevcr 265
Cdd:cd14131   156 TTSIVR---DSQVGTLNYMSPEAI-KDTSASGEGKPKskigrpSDVWSLGCILYQMVYGKTPF-QHI------------- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 266 VCQNKLFESIQEGKYE--FPDKDwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14131   218 TNPIAKLQAIIDPNHEieFPDIP----NPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
43-321 1.13e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 104.30  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSiLA 122
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQ-HPNVVEMYKSYLVGEELWVLMEYLQGGA-LT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnsCTPIT--TPEL 200
Cdd:cd06659   107 DIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR---VKLSDFGF---------CAQISkdVPKR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgevcrvcQNKLFESIQEGKY 280
Cdd:cd06659   175 KSLVGTPYWMAPEVI-----SRCPYGTEVDIWSLGIMVIEMVDGEPPYF------------------SDSPVQAMKRLRD 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 281 EFPD--KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06659   232 SPPPklKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
41-302 1.23e-25

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 105.86  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVqGAVSLQNGKE-YAVKIIEKQAGHSRSRV--FREVETLY---QCQGnknILELIEFFEDDTRFYLVFEK 114
Cdd:cd05624    78 KVIGRGAFGEV-AVVKMKNTERiYAMKILNKWEMLKRAETacFREERNVLvngDCQW---ITTLHYAFQDENYLYLVMDY 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNNSCT 193
Cdd:cd05624   154 YVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN---GHIRLADF--GSCLKMNDDGT 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTPcgsaEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdRGEVCRvcqnklfe 273
Cdd:cd05624   229 VQSSVAVGTP----DYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVET---YGKIMN-------- 293
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1358101401 274 siQEGKYEFPdkdwAHI---SSEAKDLISKLL 302
Cdd:cd05624   294 --HEERFQFP----SHVtdvSEEAKDLIQRLI 319
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
43-320 1.30e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 102.93  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKqaGHS-RSRVFREVETlYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd14662     8 IGSGNFGVARLMRNKETKELVAVKYIER--GLKiDENVQREIIN-HRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCE-SPekvSP-VKICDFDLGSGMKLNNSctPITTpe 199
Cdd:cd14662    85 ERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgSP---APrLKICDFGYSKSSVLHSQ--PKST-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 lttpCGSAEYMAPEVVevftdQATFYD-KRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgEVCRVCQN--KLFESIQ 276
Cdd:cd14662   158 ----VGTPAYIAPEVL-----SRKEYDgKVADVWSCGVTLYVMLVGAYPF-------------EDPDDPKNfrKTIQRIM 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 277 EGKYEFPdkDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14662   216 SVQYKIP--DYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
43-320 1.94e-25

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 103.41  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVF--REVETLYQCQgNKNILELIE------FFEDDTRFYLVFE- 113
Cdd:cd07840     7 IGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITaiREIKLLQKLD-HPNVVRLKEivtskgSAKYKGSIYMVFEy 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 ---KLQGgsILAHiqKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVspVKICDFDLGSGMKLNN 190
Cdd:cd07840    86 mdhDLTG--LLDN--PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINN-DGV--LKLADFGLARPYTKEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 S--CTP--IT----TPELTTpcGSAEYmAPEVvevftdqatfydkrcDLWSLGVVLYIMLSGYPPFvghCGAD------- 255
Cdd:cd07840   159 NadYTNrvITlwyrPPELLL--GATRY-GPEV---------------DMWSVGCILAELFTGKPIF---QGKTeleqlek 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 256 ----CG------WDrgEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07840   218 ifelCGspteenWP--GVSDLPWFENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
54-320 2.03e-25

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 102.12  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  54 AVSLQNGKEYAVKIIEKQAGHSRSRVFrevetlYQCQGNKNILELIEFFEDDTRFYLVFEKlQGGSILAHIQKQKHFNER 133
Cdd:cd13976    12 CVDIHTGEELVCKVVPVPECHAVLRAY------FRLPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLREP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 134 EASRVVRDVAAALDFLHTKGIAHRDLKpeniLCE---SPEKVSPVKIcdfdlgsgMKLNNSCtpITTPE---LTTPCGSA 207
Cdd:cd13976    85 EAARLFRQIASAVAHCHRNGIVLRDLK----LRKfvfADEERTKLRL--------ESLEDAV--ILEGEddsLSDKHGCP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 208 EYMAPEVVevfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHCGADCgwdrgevcrvcqnKLFESIQEGKYEFPdkdw 287
Cdd:cd13976   151 AYVSPEIL---NSGATYSGKAADVWSLGVILYTMLVGRYPF--HDSEPA-------------SLFAKIRRGQFAIP---- 208
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1358101401 288 AHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd13976   209 ETLSPRARCLIRSLLRREPSERLTAEDILLHPW 241
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-322 2.25e-25

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 102.62  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIekqaghSRSRVFR------------EVETLYQC---QGNKNILELIEFFEDDT 106
Cdd:cd14101     7 LLGKGGFGTVYAGHRISDGLQVAIKQI------SRNRVQQwsklpgvnpvpnEVALLQSVgggPGHRGVIRLLDWFEIPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEK-LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSG 185
Cdd:cd14101    81 GFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDL--RTGDIKLIDF--GSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 MKLNNSctPITTPElttpcGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwDRGevcr 265
Cdd:cd14101   157 ATLKDS--MYTDFD-----GTRVYSPPEWIL----YHQYHALPATVWSLGILLYDMVCGDIPF----------ERD---- 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 266 vcqnklfESIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14101   212 -------TDILKAKPSFN----KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
43-331 4.55e-25

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 103.49  E-value: 4.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR------FYLVFEK 114
Cdd:cd07880    23 VGSGAYGTVCSALDRRTGAKVAIKKLYRpfQSELFAKRAYRELRLLKHMK-HENVIGLLDVFTPDLSldrfhdFYLVMPF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LqgGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSGmklnn 190
Cdd:cd07880   102 M--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAvnedCE-------LKILDFGLARQ----- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 sctpiTTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRGE 262
Cdd:cd07880   168 -----TDSEMTGYVVTRWYRAPEVILNWMH----YTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDqlmeimkvTGTPSKE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 263 VCRVCQNKLFESIQEGKYEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPWVqgEQQHNGPD 331
Cdd:cd07880   239 FVQKLQSEDAKNYVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYF--EEFHDPED 309
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
41-318 7.45e-25

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 101.59  E-value: 7.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFF-----EDDTRFYLVFEKL 115
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSanrsgNGVYEVLLLMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQK--QKHFNEREASRVVRDVAAALDFLHT--KGIAHRDLKPENILCESPEKvspVKICDFdlGSgmklnnS 191
Cdd:cd14037    89 KGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGN---YKLCDF--GS------A 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTPELTTPCGSAE----------YMAPEVVEVFTDQATfyDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrG 261
Cdd:cd14037   158 TTKILPPQTKQGVTYVEedikkyttlqYRAPEMIDLYRGKPI--TEKSDIWALGCLLYKLCFYTTPF------------E 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 262 EVCRVcqnklfeSIQEGKYEFPdkDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14037   224 ESGQL-------AILNGNFTFP--DNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
43-319 8.61e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 101.45  E-value: 8.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-----AGHSRSRVFREVETLYQCqgnKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKrikkkKGETMALNEKIILEKVSS---PFIVSLAYAFETKDKLCLVLTLMNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLNnscTPI 195
Cdd:cd05577    78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---DDHGHVRISDLGLAVEFKGG---KKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 ttpelTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwDRGEvcRVCQNKLFESI 275
Cdd:cd05577   152 -----KGRVGTHGYMAPEVLQ----KEVAYDFSVDWFALGCMLYEMIAGRSPFR---------QRKE--KVDKEELKRRT 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 276 QEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHP 319
Cdd:cd05577   212 LEMAVEYPDS----FSPEARSLCEGLLQKDPERRLgcrggSADEVKEHP 256
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
54-320 1.69e-24

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 99.73  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  54 AVSLQNGKEYAVKIIEkqaghsrSRVFREVETLYQCQG-NKNILELIEFFEDDTRFYLVFEKlQGGSILAHIQKQKHFNE 132
Cdd:cd14022    12 AVHLHSGEELVCKVFD-------IGCYQESLAPCFCLPaHSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKKLRE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 133 REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLGSGMKLNNSctpittpELTTPCGSAEYMAP 212
Cdd:cd14022    84 EEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYILRGHDD-------SLSDKHGCPAYVSP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 213 EVVEVftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHcgadcgwdrgevcRVCQNKLFESIQEGKYEFPDKdwahISS 292
Cdd:cd14022   156 EILNT---SGSYSGKAADVWSLGVMLYTMLVGRYPF--H-------------DIEPSSLFSKIRRGQFNIPET----LSP 213
                         250       260
                  ....*....|....*....|....*...
gi 1358101401 293 EAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14022   214 KAKCLIRSILRREPSERLTSQEILDHPW 241
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
36-320 2.17e-24

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 99.67  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKqAGHSRSRVFREVETlYQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14665     2 YELVKDI-GSGNFGVARLMRDKQTKELVAVKYIER-GEKIDENVQREIIN-HRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCE-SPekvSP-VKICDFDLGSGMKLNnsct 193
Cdd:cd14665    79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgSP---APrLKICDFGYSKSSVLH---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 piTTPELTTpcGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgADCGWDRGevcrvcQNKLFE 273
Cdd:cd14665   152 --SQPKSTV--GTPAYIAPEVLL----KKEYDGKIADVWSCGVTLYVMLVGAYPF-----EDPEEPRN------FRKTIQ 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 274 SIQEGKYEFPdkDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14665   213 RILSVQYSIP--DYVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
41-322 2.19e-24

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 100.57  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSi 120
Cdd:cd06655    25 EKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELK-NPNIVNFLDSFLVGDELFVVMEYLAGGS- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCTPItTPEL 200
Cdd:cd06655   103 LTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGF---------CAQI-TPEQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 ---TTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqNKLFESIQE 277
Cdd:cd06655   170 skrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMVEGEPPYLNENPL--------------RALYLIATN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 278 GKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06655   231 GTPELQNPE--KLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
35-317 3.21e-24

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 99.27  E-value: 3.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLTSELlGEGAYAKVQGAVSLQNGKEYAVK---IIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 111
Cdd:cd08224     1 NYEIEKKI-GKGQFSVVYRARCLLDGRLVALKkvqIFEMMDAKARQDCLKEIDLLQQLN-HPNIIKYLASFIENNELNIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGG---SILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMk 187
Cdd:cd08224    79 LELADAGdlsRLIKHFKKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV---VKLGDLGLGRFF- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 lnNSCTPITTPELTTPCgsaeYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVC 267
Cdd:cd08224   155 --SSKTTAAHSLVGTPY----YMSPERI-----REQGYDFKSDIWSLGCLLYEMAALQSPFYG--------EKMNLYSLC 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 268 QNklfesIQEGKYE-FPDkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd08224   216 KK-----IEKCEYPpLPA---DLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
38-316 4.38e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 99.24  E-value: 4.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ---AGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14187    10 VRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSlllKPHQKEKMSMEI-AIHRSLAHQHVVGFHGFFEDNDFVYVVLEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEkvspVKICDFDLGSGMKLNNSct 193
Cdd:cd14187    89 CRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLfLNDDME----VKIGDFGLATKVEYDGE-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pittpELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFE 273
Cdd:cd14187   163 -----RKKTLCGTPNYIAPEVL-----SKKGHSFEVDIWSIGCIMYTLLVGKPPFETS---------------CLKETYL 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 274 SIQEGKYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVL 316
Cdd:cd14187   218 RIKKNEYSIP----KHINPVAASLIQKMLQTDPTARPTINELL 256
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
35-322 4.80e-24

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 99.35  E-value: 4.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLtselLGEGAYAKVQGAVSLQNGKEYAVKIIEK---QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLV 111
Cdd:cd05605     4 QYRV----LGKGGFGEVCACQVRATGKMYACKKLEKkriKKRKGEAMALNEKQILEKVN-SRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICdfDLGSGMKLN 189
Cdd:cd05605    79 LTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDD---HGHVRIS--DLGLAVEIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTpittpeLTTPCGSAEYMAPEVVEvfTDQATFydkRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdRGEvcRVCQN 269
Cdd:cd05605   154 EGET------IRGRVGTVGYMAPEVVK--NERYTF---SPDWWGLGCLIYEMIEGQAPFRA---------RKE--KVKRE 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 270 KLFESIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQ 322
Cdd:cd05605   212 EVDRRVKEDQEEYSEK----FSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFK 265
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
43-324 5.15e-24

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 99.42  E-value: 5.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKII--------EKQaghsrsrVFREVETLYQCQgNKNILELIEFF--EDDTRFYLVF 112
Cdd:cd06621     9 LGEGAGGSVTKCRLRNTKTIFALKTIttdpnpdvQKQ-------ILRELEINKSCA-SPYIVKYYGAFldEQDSSIGIAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVA----AALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgSGmKL 188
Cdd:cd06621    81 EYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAesvlKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCDFGV-SG-EL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNSCTpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrGEVcRVCQ 268
Cdd:cd06621   156 VNSLA-------GTFTGTSYYMAPERI-----QGGPYSITSDVWSLGLTLLEVAQNRFPFPPE---------GEP-PLGP 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 269 NKLFESIQEGK-YEFPDKDWAHI--SSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd06621   214 IELLSYIVNMPnPELKDEPENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQ 272
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
43-322 5.90e-24

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 99.34  E-value: 5.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSiLA 122
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYH-HENVVDMYNSYLVGDELWVVMEFLEGGA-LT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnsCTPIT--TPEL 200
Cdd:cd06658   108 DIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR---IKLSDFGF---------CAQVSkeVPKR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgevcrvcQNKLFESIQEGKY 280
Cdd:cd06658   176 KSLVGTPYWMAPEVISRLP-----YGTEVDIWSLGIMVIEMIDGEPPYF------------------NEPPLQAMRRIRD 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 281 EFPD--KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06658   233 NLPPrvKDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLK 276
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
41-323 6.53e-24

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 101.25  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVqGAVSLQNG-KEYAVKIIEKQAGHSRSRV--FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05623    78 KVIGRGAFGEV-AVVKLKNAdKVFAMKILNKWEMLKRAETacFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNNSCTPIT 196
Cdd:cd05623   157 GDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMN---GHIRLADF--GSCLKLMEDGTVQS 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPELTTPcgsaEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdRGEVCRvcqnklfesiQ 276
Cdd:cd05623   232 SVAVGTP----DYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVET---YGKIMN----------H 294
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 277 EGKYEFPDKdWAHISSEAKDLISKLLVrDAKQRLSAAQV---LQHPWVQG 323
Cdd:cd05623   295 KERFQFPTQ-VTDVSENAKDLIRRLIC-SREHRLGQNGIedfKNHPFFVG 342
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
123-318 7.74e-24

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 99.02  E-value: 7.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSPVKICDFDLGSgmKLNNSctpitTPELTT 202
Cdd:cd13974   122 YVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLN--KRTRKITITNFCLGK--HLVSE-----DDLLKD 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRgevcrvCQNKLFESIQEGKYEF 282
Cdd:cd13974   193 QRGSPAYISPDVLS----GKPYLGKPSDMWALGVVLFTMLYGQFPF---------YDS------IPQELFRKIKAAEYTI 253
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1358101401 283 PDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd13974   254 PED--GRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
39-321 7.96e-24

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 98.89  E-value: 7.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  39 TSELLGEGAYAKVQGAVSLQNGKEYAVK---IIEKQAGHSRSRVfREVETLYQCQ--GNKNILELIEFF-----EDDTRF 108
Cdd:cd07838     3 EVAEIGEGAYGTVYKARDLQDGRFVALKkvrVPLSEEGIPLSTI-REIALLKQLEsfEHPNVVRLLDVChgprtDRELKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEklqggsilaHIQK------QKH----FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKIC 178
Cdd:cd07838    82 TLVFE---------HVDQdlatylDKCpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ---VKLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFDLGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVEvftdQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgw 258
Cdd:cd07838   150 DFGLARIYSFEMALTSVVV--------TLWYRAPEVLL----QSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEAD--- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 259 drgevcrvcQ-NKLFESI-QEGKYEFPD------------------KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd07838   214 ---------QlGKIFDVIgLPSEEEWPRnsalprssfpsytprpfkSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284

                  ...
gi 1358101401 319 PWV 321
Cdd:cd07838   285 PYF 287
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
32-319 9.24e-24

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 97.87  E-value: 9.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFY 109
Cdd:cd08529     2 FEILNKL-----GKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMReeAIDEARVLSKLN-SPYVIKYYDSFVDKGKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQ--KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvKICDfdLGSGMK 187
Cdd:cd08529    76 IVMEYAENGDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNV---KIGD--LGVAKI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNsctpiTTPELTTPCGSAEYMAPEVVEvftDQAtfYDKRCDLWSLGVVLYIMLSGYPPF-VGHCGAdcgwdrgevcrv 266
Cdd:cd08529   151 LSD-----TTNFAQTIVGTPYYLSPELCE---DKP--YNEKSDVWALGCVLYELCTGKHPFeAQNQGA------------ 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 267 cqnkLFESIQEGKYE-FPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08529   209 ----LILKIVRGKYPpIS----ASYSQDLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
41-309 1.03e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 98.34  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKE-YAVKII----------EKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFY 109
Cdd:cd08528     6 ELLGSGAFGCVYKVRKKSNGQTlLALKEInmtnpafgrtEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLENDRLY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHI----QKQKHFNEREASRVVRDVAAALDFLHT-KGIAHRDLKPENILCESPEKVSpvkICDFDLGS 184
Cdd:cd08528    86 IVMELIEGAPLGEHFsslkEKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVT---ITDFGLAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 185 gMKLNNSctpittPELTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevc 264
Cdd:cd08528   163 -QKGPES------SKMTSVVGTILYSCPEIVQNEP-----YGEKADIWALGCILYQMCTLQPPFYST------------- 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 265 rvCQNKLFESIQEGKYE-FPDKDWahiSSEAKDLISKLLVRDAKQR 309
Cdd:cd08528   218 --NMLTLATKIVEAEYEpLPEGMY---SDDITFVIRSCLTPDPEAR 258
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
43-248 1.61e-23

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 97.12  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVslQNGKEYAVKIIEKQAghSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI-- 120
Cdd:cd14058     1 VGRGSFGVVCKAR--WRNQIVAVKIIESES--EKKAFEVEVRQLSRVD-HPNIIKLYGACSNQKPVCLVMEYAEGGSLyn 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQK-HFNEREASRVVRDVAAALDFLHT---KGIAHRDLKPENILCESPEKVspVKICDFDLGSGMKLNnsctpit 196
Cdd:cd14058    76 VLHGKEPKpIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTV--LKICDFGTACDISTH------- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 197 tpeLTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14058   147 ---MTNNKGSAAWMAPEVFE-----GSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
42-319 1.76e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 97.76  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05631     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgeAMALNEKRILEKVN-SRFVVSLAYAYETKDALCLVLTIMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGsgmklnnsctpIT 196
Cdd:cd05631    86 DLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDD---RGHIRISDLGLA-----------VQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPELTT---PCGSAEYMAPEVVEvfTDQATFYDkrcDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEVCRVCQNKLFE 273
Cdd:cd05631   152 IPEGETvrgRVGTVGYMAPEVIN--NEKYTFSP---DWWGLGCLIYEMIQGQSPF-----------RKRKERVKREEVDR 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 274 SIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHP 319
Cdd:cd05631   216 RVKEDQEEYSEK----FSEDAKSICRMLLTKNPKERLgcrgnGAAGVKQHP 262
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
41-320 1.79e-23

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 97.88  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGg 118
Cdd:cd07846     7 GLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKkiAMREIKMLKQLR-HENLVNLIEVFRRKKRWYLVFEFVDH- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMklnNSCTPITT 197
Cdd:cd07846    85 TVLDDLEKYPNgLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV-SQSGV--VKLCDFGFARTL---AAPGEVYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 PELTTpcgsAEYMAPEVveVFTDqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD-------CgwdRGEVCR----- 265
Cdd:cd07846   159 DYVAT----RWYRAPEL--LVGD--TKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDqlyhiikC---LGNLIPrhqel 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 266 VCQNKLFE-----SIQEgkYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07846   228 FQKNPLFAgvrlpEVKE--VEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
46-330 1.80e-23

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 99.18  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  46 GAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVfrevetlYQCQGNKNILEL------IEFF---EDDTRFYLVFEKLQ 116
Cdd:cd05610    15 GAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMV-------HQVQAERDALALskspfiVHLYyslQSANNVYLVMEYLI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgSGMKLN---NSCT 193
Cdd:cd05610    88 GGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE---GHIKLTDFGL-SKVTLNrelNMMD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTP--------------------------------------------CGSAEYMAPEVVevftdQATFYDKRC 229
Cdd:cd05610   164 ILTTPSMAKPkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegeriLGTPDYLAPELL-----LGKPHGPAV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 230 DLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqnKLFESIQEGKYEFPDKDWAhISSEAKDLISKLLVRDAKQR 309
Cdd:cd05610   239 DWWALGVCLFEFLTGIPPFNDETPQ---------------QVFQNILNRDIPWPEGEEE-LSVNAQNAIEILLTMDPTKR 302
                         330       340
                  ....*....|....*....|....
gi 1358101401 310 LSAAQVLQHPWVQG---EQQHNGP 330
Cdd:cd05610   303 AGLKELKQHPLFHGvdwENLQNQT 326
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
42-248 1.86e-23

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 98.65  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrsrVFREVETLYQCQGNKNILE----------LIEFFEDDTRFYLV 111
Cdd:cd05588     2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKE-------LVNDDEDIDWVQTEKHVFEtasnhpflvgLHSCFQTESRLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMklnns 191
Cdd:cd05588    75 IEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSE---GHIKLTDY----GM----- 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 192 CTPITTPELTTP--CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd05588   143 CKEGLRPGDTTStfCGTPNYIAPEIL-----RGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
43-321 1.90e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 97.19  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIE--KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd08218     8 IGEGSFGKALLVKSKEDGKQYVIKEINisKMSPKEREESRKEVAVLSKMK-HPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQK--HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDFdlGSGMKLNNsctpitTP 198
Cdd:cd08218    87 YKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDF--GIARVLNS------TV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPC-GSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgaDCGWDRGEVCRvcqnklfesIQE 277
Cdd:cd08218   156 ELARTCiGTPYYLSPEICE-----NKPYNNKSDIWALGCVLYEMCTLKHAF------EAGNMKNLVLK---------IIR 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 278 GKY-EFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd08218   216 GSYpPVP----SRYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
42-319 2.11e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 97.79  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05630     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgeAMALNEKQILEKVN-SRFVVSLAYAYETKDALCLVLTLMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGsgmklnnsctpIT 196
Cdd:cd05630    86 DLKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLA-----------VH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPELTT---PCGSAEYMAPEVVEvfTDQATFYDkrcDLWSLGVVLYIMLSGYPPFVGHcgaDCGWDRGEVCRVcqnklfe 273
Cdd:cd05630   152 VPEGQTikgRVGTVGYMAPEVVK--NERYTFSP---DWWALGCLLYEMIAGQSPFQQR---KKKIKREEVERL------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 274 sIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHP 319
Cdd:cd05630   217 -VKEVPEEYSEK----FSPQARSLCSMLLCKDPAERLgcrggGAREVKEHP 262
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
41-322 2.32e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 97.87  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSi 120
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgsgmklnnsCTPItTPEL 200
Cdd:cd06654   104 LTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGF---------CAQI-TPEQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 ---TTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqNKLFESIQE 277
Cdd:cd06654   171 skrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMIEGEPPYLNENPL--------------RALYLIATN 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 278 GKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06654   232 GTPELQNPE--KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
42-325 3.79e-23

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 98.57  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR---VFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05618    27 VIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDidwVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMklnnsCTPITTP 198
Cdd:cd05618   107 DLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE---GHIKLTDY----GM-----CKEGLRP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTP--CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvGHCGADCGWDRGevcrvCQNKLFESIQ 276
Cdd:cd05618   175 GDTTStfCGTPNYIAPEIL-----RGEDYGFSVDWWALGVLMFEMMAGRSPF-DIVGSSDNPDQN-----TEDYLFQVIL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 277 EGKYEFPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQ 325
Cdd:cd05618   244 EKQIRIPRS----LSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHP 288
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
41-321 5.00e-23

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 97.23  E-value: 5.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVfrEVETLYQCQ-----GNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14210    19 SVLGKGSFGQVVKCLDHKTGQLVAIKIIRnKKRFHQQALV--EVKILKHLNdndpdDKHNIVRYKDSFIFRGHLCIVFEL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LqGGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpVKICDFdlGSGMKLNN-S 191
Cdd:cd14210    97 L-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSS-IKVIDF--GSSCFEGEkV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITtpelttpcgSAEYMAPEVVevftdqatF---YDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGE-VCRVC 267
Cdd:cd14210   173 YTYIQ---------SRFYRAPEVI--------LglpYDTAIDMWSLGCILAELYTGYPLFPGE-------NEEEqLACIM 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 268 Q----------------NKLFES--------IQEGKYEFPD-KDWAHISSEAK----DLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14210   229 EvlgvppkslidkasrrKKFFDSngkprpttNSKGKKRRPGsKSLAQVLKCDDpsflDFLKKCLRWDPSERMTPEEALQH 308

                  ...
gi 1358101401 319 PWV 321
Cdd:cd14210   309 PWI 311
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
103-250 2.03e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.94  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 EDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICD 179
Cdd:NF033483   77 EDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL------ITKdgrVKVTD 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 180 FdlGSGMKLNNSCTPITTPELttpcGSAEYMAPEvvevftdQAT--FYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:NF033483  151 F--GIARALSSTTMTQTNSVL----GTVHYLSPE-------QARggTVDARSDIYSLGIVLYEMLTGRPPFDG 210
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
33-317 2.67e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 97.01  E-value: 2.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSeLLGEGAYAKVQGAVSLQNGKEYAV-KII----EKQAGHSRSrvfrEVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:PTZ00267   66 EHMYVLTT-LVGRNPTTAAFVATRGSDPKEKVVaKFVmlndERQAAYARS----ELHCLAACD-HFGIVKHFDDFKSDDK 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQK--QKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlG 183
Cdd:PTZ00267  140 LLLIMEYGSGGDLNKQIKQrlKEHlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL-MPTGI--IKLGDF--G 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMKLNNSctpITTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgev 263
Cdd:PTZ00267  215 FSKQYSDS---VSLDVASSFCGTPYYLAPELWE-----RKRYSKKADMWSLGVILYELLTLHRPFKGP------------ 274
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 264 crvCQNKLFESIQEGKYE-FPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:PTZ00267  275 ---SQREIMQQVLYGKYDpFP----CPVSSGMKALLDPLLSKNPALRPTTQQLLH 322
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
41-320 3.52e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 94.56  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII------EKQAGHSRSrVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd07841     6 KKLGEGTYAVVYKARDKETGRIVAIKKIklgerkEAKDGINFT-ALREIKLLQELK-HPNIIGLLDVFGHKSNINLVFEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGsiLAHIQKQKHFNEREAsrvvrDVAA-------ALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDL----G 183
Cdd:cd07841    84 METD--LEKVIKDKSIVLTPA-----DIKSymlmtlrGLEYLHSNWILHRDLKPNNLLI-ASDGV--LKLADFGLarsfG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 184 SGMKlnnsctpITTPELTTPCgsaeYMAPEVveVFTdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgaDCGWDR-GE 262
Cdd:cd07841   154 SPNR-------KMTHQVVTRW----YRAPEL--LFG--ARHYGVGVDMWSVGCIFAELLLRVPFLPG----DSDIDQlGK 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 263 VCRVC---------QNKLFESIQEGKyEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07841   215 IFEALgtpteenwpGVTSLPDYVEFK-PFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
43-319 4.68e-22

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 94.15  E-value: 4.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKI---IEKQaghsrsRVFREVETLYQCQGNKNILELIE-FFEDDTRFY-LVFEKLQG 117
Cdd:cd14132    26 IGRGKYSEVFEGINIGNNEKVVIKVlkpVKKK------KIKREIKILQNLRGGPNIVKLLDvVKDPQSKTPsLIFEYVNN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKqkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvsPVKICDFDLGsgmklnnsctpitt 197
Cdd:cd14132   100 TDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKR--KLRLIDWGLA-------------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 pELTTP-------CGSAEYMAPEV-VEVFtdqatFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadCGWDRGE----VCR 265
Cdd:cd14132   161 -EFYHPgqeynvrVASRYYKGPELlVDYQ-----YYDYSLDMWSLGCMLASMIFRKEPFF------HGHDNYDqlvkIAK 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 266 VC-QNKLFESIQegKY-------------EFPDKDWAH---------ISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14132   229 VLgTDDLYAYLD--KYgielpprlndilgRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
26-321 4.94e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 93.92  E-value: 4.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  26 DSLPGKfEDMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQagHSrsrVFREVETLYqcqgnkNILELIE----- 100
Cdd:cd06638    11 DSFPDP-SDTWEII-ETIGKGTYGKVFKVLNKKNGSKAAVKILDPI--HD---IDEEIEAEY------NILKALSdhpnv 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 101 ------FFEDDT----RFYLVFEKLQGGSIL----AHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC 166
Cdd:cd06638    78 vkfygmYYKKDVkngdQLWLVLELCNGGSVTdlvkGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 167 ESPekvSPVKICDFdlGSGMKLNNsctpiTTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYP 246
Cdd:cd06638   158 TTE---GGVKLVDF--GVSAQLTS-----TRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDP 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 247 PFvghcgADCGWDRGeVCRVCQNKlfesiqEGKYEFPDKdWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06638   228 PL-----ADLHPMRA-LFKIPRNP------PPTLHQPEL-W---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
43-321 7.90e-22

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 92.86  E-value: 7.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVK-IIEKQAGHSRSrvFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSiL 121
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKeIPERDSREVQP--LHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGS-L 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQK----HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFdlGSGMKLN--NSCTpi 195
Cdd:cd06624    93 SALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGV--VKISDF--GTSKRLAgiNPCT-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 ttpelTTPCGSAEYMAPEVVevftDQATF-YDKRCDLWSLGVVLYIMLSGYPPFVghcgaDCGWDRGEVCRVCQNKLFES 274
Cdd:cd06624   167 -----ETFTGTLQYMAPEVI----DKGQRgYGPPADIWSLGCTIIEMATGKPPFI-----ELGEPQAAMFKVGMFKIHPE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 275 IqegkyefPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06624   233 I-------PES----LSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
42-322 9.31e-22

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 93.88  E-value: 9.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05632     9 VLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRkgeSMALNEKQILEKVN-SQFVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGsgmklnnsctpIT 196
Cdd:cd05632    88 DLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDD---YGHIRISDLGLA-----------VK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TPE---LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdRGEVCRVCQNKLFE 273
Cdd:cd05632   154 IPEgesIRGRVGTVGYMAPEVL-----NNQRYTLSPDYWGLGCLIYEMIEGQSPF-----------RGRKEKVKREEVDR 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 274 SIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQ 322
Cdd:cd05632   218 RVLETEEVYSAK----FSEEAKSICKMLLTKDPKQRLgcqeeGAGEVKRHPFFR 267
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
42-319 1.02e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 92.49  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd08220     7 VVGRGAYGTVYLCRRKDDNKLVIIKQIpvEQMTKEERQAALNEVKVL-SMLHHPNIIEYYESFLEDKALMIVMEYAPGGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFdlGSGMKLNNSCTPITT 197
Cdd:cd08220    86 LFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV--VKIGDF--GISKILSSKSKAYTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 peLTTPCgsaeYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdrgevcrvcQN--KLFESI 275
Cdd:cd08220   162 --VGTPC----YISPELCE-----GKPYNQKSDIWALGCVLYELASLKRAFEA-----------------ANlpALVLKI 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 276 QEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08220   214 MRGTFAPISDRY---SEELRHLILSMLHLDPNKRPTLSEIMAQP 254
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
81-319 1.10e-21

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 92.42  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  81 REVETLYQCQgNKNILELIEF------FEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGI 154
Cdd:cd14012    47 KELESLKKLR-HPNLVSYLAFsierrgRSDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 155 AHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPElttpcgSAEYMAPEVvevfTDQATFYDKRCDLWSL 234
Cdd:cd14012   126 VHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDEFK------QTYWLPPEL----AQGSKSPTRKTDVWDL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 235 GVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnklfesiqegkyefPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQ 314
Cdd:cd14012   196 GLLFLQMLFGLDVLEKYTSPN---------------------------PVLVSLDLSASLQDFLSKCLSLDPKKRPTALE 248

                  ....*
gi 1358101401 315 VLQHP 319
Cdd:cd14012   249 LLPHE 253
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
43-321 1.13e-21

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 93.16  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSiLA 122
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGA-LT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnsCTPIT--TPEL 200
Cdd:cd06657   106 DIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGF---------CAQVSkeVPRR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 201 TTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgevcrvcQNKLFESIQEGKY 280
Cdd:cd06657   174 KSLVGTPYWMAPELISRLP-----YGPEVDIWSLGIMVIEMVDGEPPYF------------------NEPPLKAMKMIRD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 281 EFPD--KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06657   231 NLPPklKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
42-320 1.23e-21

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 93.81  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR------FYLVFE 113
Cdd:cd07879    22 QVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfQSEIFAKRAYRELTLLKHMQ-HENVIGLLDVFTSAVSgdefqdFYLVMP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQG--GSILAHiqkqkHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSGmk 187
Cdd:cd07879   101 YMQTdlQKIMGH-----PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAvnedCE-------LKILDFGLARH-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 lnnsctpiTTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWD 259
Cdd:cd07879   167 --------ADAEMTGYVVTRWYRAPEVILNWMH----YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDqltqilkvTGVP 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 260 RGEVCRVCQNKLFESIQEGKYEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07879   235 GPEFVQKLEDKAAKSYIKSLPKYPRKDFSTLfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPY 299
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
41-250 1.33e-21

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 92.17  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QG---AVSLQNGKEYAVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:pfam07714   5 EKLGEGAFGEVyKGtlkGEGENTKIKVAVKTLKEGADEEEREDFlEEASIMKKLD-HPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlgsGMklnnsCTP 194
Cdd:pfam07714  84 PGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV---VKISDF----GL-----SRD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 195 ITTPELTTPCGSAE----YMAPEVVE--VFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:pfam07714 152 IYDDDYYRKRGGGKlpikWMAPESLKdgKFTSKS-------DVWSFGVLLWEIFTlGEQPYPG 207
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
41-321 1.76e-21

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 92.11  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQnGKEYAVKIIEKQAGHSRS------RVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd06631     7 NVLGKGAYGTVYCGLTST-GQLIAVKQVELDTSDKEKaekeyeKLQEEVDLLKTLK-HVNIVGYLGTCLEDNVVSIFMEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFdlGSGMKLNNSCTP 194
Cdd:cd06631    85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML-MPNGV--IKLIDF--GCAKRLCINLSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPE-LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcGAD---------CGWDRGEVC 264
Cdd:cd06631   160 GSQSQlLKSMRGTPYWMAPEVI-----NETGHGRKSDIWSIGCTVFEMATGKPP-----WADmnpmaaifaIGSGRKPVP 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 265 RVcqnklfesiqegkyefPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06631   230 RL----------------PD----KFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
41-321 1.89e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 91.56  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd08225     6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIdlTKMPVKEKEASKKEVILLAKMK-HPNIVTFFASFQENGRLFIVMEYCDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvKICDFdlGSGMKLNNSCtpit 196
Cdd:cd08225    85 DLMKRINRQRGvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVA--KLGDF--GIARQLNDSM---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpELTTPC-GSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCgwdrgeVCRVCQNKlFESI 275
Cdd:cd08225   157 --ELAYTCvGTPYYLSPEIC-----QNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQL------VLKICQGY-FAPI 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 276 QegkyefpdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd08225   223 S-----------PNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
43-321 2.23e-21

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 93.02  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS--RSRVFREVETLYQCQgNKNILELIEFF----EDdtrFYLVFEKLq 116
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPvlAKRTYRELKLLKHLR-HENIISLSDIFisplED---IYFVTELL- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 gGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSgmklnnsc 192
Cdd:cd07856    93 -GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILvnenCD-------LKICDFGLAR-------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 tpITTPELTTPCGSAEYMAPEVveVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVG--HCGADC------GWDRGEVC 264
Cdd:cd07856   157 --IQDPQMTGYVSTRYYRAPEI--MLTWQK--YDVEVDIWSAGCIFAEMLEGKPLFPGkdHVNQFSiitellGTPPDDVI 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 265 R-VCQNKLFESIQegkyEFPDKDWAHISS-------EAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07856   231 NtICSENTLRFVQ----SLPKRERVPFSEkfknadpDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
41-321 2.99e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 91.26  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIekQAGHSRSRVFREVETLyQC--QGNKNILE--LIEFF-----EDDTRFYLV 111
Cdd:cd06652     8 KLLGQGAFGRVYLCYDADTGRELAVKQV--QFDPESPETSKEVNAL-ECeiQLLKNLLHerIVQYYgclrdPQERTLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFdlGSGMKLNNS 191
Cdd:cd06652    85 MEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDS---VGNVKLGDF--GASKRLQTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTPELTTpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVcrvcQNKL 271
Cdd:cd06652   160 CLSGTGMKSVT--GTPYWMSPEVI-----SGEGYGRKADIWSVGCTVVEMLTEKPP----------WAEFEA----MAAI 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 272 FE-SIQEGKYEFPdkdwAHISSEAKDLISKLLVrDAKQRLSAAQVLQHPWV 321
Cdd:cd06652   219 FKiATQPTNPQLP----AHVSDHCRDFLKRIFV-EAKLRPSADELLRHTFV 264
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
36-320 3.31e-21

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 92.24  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSeLLGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQ-----GNKNILELIEFFEDDTRFYL 110
Cdd:cd14134    14 YKILR-LLGEGTFGKVLECWDRKRKRYVAVKII-RNVEKYREAAKIEIDVLETLAekdpnGKSHCVQLRDWFDYRGHMCI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLqGGSI-------------LAHIQKqkhfnereasrVVRDVAAALDFLHTKGIAHRDLKPENILCESPE------- 170
Cdd:cd14134    92 VFELL-GPSLydflkknnygpfpLEHVQH-----------IAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynp 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 171 ---------KVSPVKICDFdlGSGMKLNNSCTPITTpelTTPcgsaeYMAPEVV-EVFTDQAtfydkrCDLWSLGVVLYI 240
Cdd:cd14134   160 kkkrqirvpKSTDIKLIDF--GSATFDDEYHSSIVS---TRH-----YRAPEVIlGLGWSYP------CDVWSIGCILVE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 241 MLSGYPPFVGHcgadcgwDRGE----VCRVC----QNKLFESIQEGKYEFPDK---DWAHISSEAK-------------- 295
Cdd:cd14134   224 LYTGELLFQTH-------DNLEhlamMERILgplpKRMIRRAKKGAKYFYFYHgrlDWPEGSSSGRsikrvckplkrlml 296
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1358101401 296 ----------DLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14134   297 lvdpehrllfDLIRKMLEYDPSKRITAKEALKHPF 331
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31-322 4.40e-21

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 92.00  E-value: 4.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSeLLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVfrEVETLYQC-----QGNKNILELIEFFED 104
Cdd:cd14226    10 KWMDRYEIDS-LIGKGSFGQVVKAYDHVEQEWVAIKIIKnKKAFLNQAQI--EVRLLELMnkhdtENKYYIVRLKRHFMF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLQGGsiLAHIQKQKHFneREAS-RVVRDVA----AALDFLHTK--GIAHRDLKPENILCESPEKvSPVKI 177
Cdd:cd14226    87 RNHLCLVFELLSYN--LYDLLRNTNF--RGVSlNLTRKFAqqlcTALLFLSTPelSIIHCDLKPENILLCNPKR-SAIKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CDFdlGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCG 257
Cdd:cd14226   162 IDF--GSSCQLGQRIYQYIQ--------SRFYRSPEVL-----LGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 258 WDRGEVCRVCQN----------KLFESIQEGKYEFPDKDWAH-------------ISSEA-------------------- 294
Cdd:cd14226   227 NKIVEVLGMPPVhmldqapkarKFFEKLPDGTYYLKKTKDGKkykppgsrklheiLGVETggpggrragepghtvedylk 306
                         330       340
                  ....*....|....*....|....*....
gi 1358101401 295 -KDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14226   307 fKDLILRMLDYDPKTRITPAEALQHSFFK 335
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
41-319 5.35e-21

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 90.36  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQ-------NGKEYAVKIIEKQAghSRSRVFREVETLYQCQGNKNILELIEFF--EDDTRFYLV 111
Cdd:cd14019     7 EKIGEGTFSSVYKAEDKLhdlydrnKGRLVALKHIYPTS--SPSRILNELECLERLGGSNNVSGLITAFrnEDQVVAVLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FeklqggsiLAHIQKQKHFNE---REASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSPVkICDFDLGSGMKl 188
Cdd:cd14019    85 Y--------IEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY-NRETGKGV-LVDFGLAQREE- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 nnsctpiTTPELTTPC-GSAEYMAPEVVEVFTDQATfydkRCDLWSLGVVLYIMLSG-YPPFVGHcgADCgwdrgevcrv 266
Cdd:cd14019   154 -------DRPEQRAPRaGTRGFRAPEVLFKCPHQTT----AIDIWSAGVILLSILSGrFPFFFSS--DDI---------- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 267 cqnklfESIQEgkyefpdkdWAHI--SSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14019   211 ------DALAE---------IATIfgSDEAYDLLDKLLELDPSKRITAEEALKHP 250
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
54-321 5.65e-21

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 89.94  E-value: 5.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  54 AVSLQNGKEYAVKIIEKQAGHsrsrvfrEVETLYQCQG-NKNILELIEFFEDDTRFYLVFEKlQGGSILAHIQKQKHFNE 132
Cdd:cd14024    12 AEHYQTEKEYTCKVLSLRSYQ-------ECLAPYDRLGpHEGVCSVLEVVIGQDRAYAFFSR-HYGDMHSHVRRRRRLSE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 133 REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKIcdfdlgsgmKLNNSCtPITTPE--LTTPCGSAEYM 210
Cdd:cd14024    84 DEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLV---------NLEDSC-PLNGDDdsLTDKHGCPAYV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 211 APEVVevfTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVCrvcqnkLFESIQEGKYEFPdkdwAHI 290
Cdd:cd14024   154 GPEIL---SSRRSYSGKAADVWSLGVCLYTMLLGRYPF---------QDTEPAA------LFAKIRRGAFSLP----AWL 211
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1358101401 291 SSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14024   212 SPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
43-320 5.77e-21

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 91.48  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVETLyQC--------QGNKNILELIEFFE----DDTRFYL 110
Cdd:cd14136    18 LGWGHFSTVWLCWDLQNKRFVALKVV-KSAQHYTEAALDEIKLL-KCvreadpkdPGREHVVQLLDDFKhtgpNGTHVCM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLqGGSILAHIqkqKHFNER-----EASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEkvSPVKICDfdlgs 184
Cdd:cd14136    96 VFEVL-GPNLLKLI---KRYNYRgiplpLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISK--IEVKIAD----- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 185 gmkLNNSCtpITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWD----- 259
Cdd:cd14136   165 ---LGNAC--WTDKHFTEDIQTRQYRSPEVI-----LGAGYGTPADIWSTACMAFELATGDYLFDPHSGEDYSRDedhla 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 260 --------------------------RGEVCRVcqNKL----FESIQEGKYEFPDKDWAHISSeakdLISKLLVRDAKQR 309
Cdd:cd14136   235 liiellgriprsiilsgkysreffnrKGELRHI--SKLkpwpLEDVLVEKYKWSKEEAKEFAS----FLLPMLEYDPEKR 308
                         330
                  ....*....|.
gi 1358101401 310 LSAAQVLQHPW 320
Cdd:cd14136   309 ATAAQCLQHPW 319
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
43-331 6.28e-21

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 92.02  E-value: 6.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRF------YLVFEK 114
Cdd:cd07877    25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRpfQSIIHAKRTYRELRLLKHMK-HENVIGLLDVFTPARSLeefndvYLVTHL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LqgGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSGmklnn 190
Cdd:cd07877   104 M--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAvnedCE-------LKILDFGLARH----- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 sctpiTTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRGE 262
Cdd:cd07877   170 -----TDDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGRTLFPGTDHIDqlklilrlVGTPGAE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 263 VCRVCQNKLFESIQEGKYEFPDKDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPWVqgeQQHNGPD 331
Cdd:cd07877   241 LLKKISSESARNYIQSLTQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYF---AQYHDPD 310
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
41-332 7.45e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 90.89  E-value: 7.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQA-GHSRSRVFREVETLYQCQGNKNILEL--IEFFEDDT-----RFYLVF 112
Cdd:cd06616    12 GEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVdEKEQKRLLMDLDVVMRSSDCPYIVKFygALFREGDCwicmeLMDISL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLqggSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCEspeKVSPVKICDFDLgSGmKLNNS 191
Cdd:cd06616    92 DKF---YKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLD---RNGNIKLCDFGI-SG-QLVDS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPittpelTTPCGSAEYMAPEVVEVFTDQATfYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcGWdrgevcrvcqNKL 271
Cdd:cd06616   164 IAK------TRDAGCRPYMAPERIDPSASRDG-YDVRSDVWSLGITLYEVATGKFPYP-------KW----------NSV 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 272 FESIQEGKYEFPDK----DWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQQHNGPDA 332
Cdd:cd06616   220 FDQLTQVVKGDPPIlsnsEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVDVA 284
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
43-317 1.32e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 89.70  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVK---IIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd08228    10 IGRGQFSEVYRATCLLDRKPVALKkvqIFEMMDAKARQDCVKEIDLLKQLN-HPNVIKYLDSFIEDNELNIVLELADAGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 I---LAHIQKQKHF-NEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGsgmKLNNSCTPI 195
Cdd:cd08228    89 LsqmIKYFKKQKRLiPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLG---RFFSSKTTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTPcgsaEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVCQNklfesI 275
Cdd:cd08228   163 AHSLVGTP----YYMSPERI-----HENGYNFKSDIWSLGCLLYEMAALQSPFYG--------DKMNLFSLCQK-----I 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 276 QEGKYefPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd08228   221 EQCDY--PPLPTEHYSEKLRELVSMCIYPDPDQRPDIGYVHQ 260
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
44-321 1.44e-20

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 89.11  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  44 GEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRsRVFREVETLYQCQGNKnILELIEFFEDDTRFYLVFEKLQGGSILAH 123
Cdd:cd14111    12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQ-GVLQEYEILKSLHHER-IMALHEAYITPRYLVLIAEFCSGKELLHS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 124 IQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFdlGSGMKLNnsctPITTPELTTP 203
Cdd:cd14111    90 LIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTN---LNAIKIVDF--GSAQSFN----PLSLRQLGRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 204 CGSAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLSGYPPFVGHcgadcgwDRGEVcrvcQNKlfesIQEGKYE 281
Cdd:cd14111   161 TGTLEYMAPEMVkgEPVGPPA-------DIWSIGVLTYIMLSGRSPFEDQ-------DPQET----EAK----ILVAKFD 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1358101401 282 fPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14111   219 -AFKLYPNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
43-331 1.77e-20

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 90.49  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK---QAGHSRsRVFREVETLYQCQgNKNILELIEFF------EDDTRFYLVFE 113
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRpfqSLIHAR-RTYRELRLLKHMK-HENVIGLLDVFtpatsiENFNEVYLVTN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLqgGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSGmkln 189
Cdd:cd07878   101 LM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAvnedCE-------LRILDFGLARQ---- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nsctpiTTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRG 261
Cdd:cd07878   168 ------ADDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLKGKALFPGNDYIDqlkrimevVGTPSP 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 262 EVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAK----DLISKLLVRDAKQRLSAAQVLQHPWVqgeQQHNGPD 331
Cdd:cd07878   238 EVLKKISSEHARKYIQSLPHMPQQDLKKIFRGANplaiDLLEKMLVLDSDKRISASEALAHPYF---SQYHDPE 308
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
42-323 1.81e-20

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 89.42  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsRSRVfREVETLyqCQGNKNILELIEF-------------FEDDTRF 108
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKK----RIKM-KQGETL--ALNERIMLSLVSTggdcpfivcmtyaFQTPDKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPE-KVSPVKI-CDFdlgSG 185
Cdd:cd05606    74 CFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANIlLDEHGHvRISDLGLaCDF---SK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 MKLNNSctpittpelttpCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwDRGEVCR 265
Cdd:cd05606   151 KKPHAS------------VGTHGYMAPEVLQ----KGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTK----DKHEIDR 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 266 VcqnklfesIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05606   211 M--------TLTMNVELPDS----FSPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPFFKG 261
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
42-316 2.07e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 88.88  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd08219     7 VVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNN----SCTPI 195
Cdd:cd08219    87 QKIklQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDF--GSARLLTSpgayACTYV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPelttpcgsaEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcGWdRGEVCRVCQnklfesi 275
Cdd:cd08219   162 GTP---------YYVPPEIWENMP-----YNNKSDIWSLGCILYELCTLKHPFQAN-----SW-KNLILKVCQ------- 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1358101401 276 qeGKYE-FPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVL 316
Cdd:cd08219   215 --GSYKpLP----SHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
41-320 2.20e-20

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 89.27  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd07835     5 EKIGEGTYGVVYKARDKLTGEIVALKKIrlETEDEGVPSTAIREISLLKELN-HPNIVRLLDVVHSENKLYLVFEFLDLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 --SILAHIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGS--GMKLNNsctp 194
Cdd:cd07835    84 lkKYMDSSPLTG-LDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLI---DTEGALKLADFGLARafGVPVRT---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 iTTPELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvcqnKLF-- 272
Cdd:cd07835   156 -YTHEVVT----LWYRAPEILL----GSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEID--------------QLFri 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 273 --------ESIQEGKYEFPD----------KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07835   213 frtlgtpdEDVWPGVTSLPDykptfpkwarQDLSKVvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
43-270 2.45e-20

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 88.66  E-value: 2.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQcQGNKNILELIEFFEDDTRFYLVFEKLQGGSi 120
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERkaLLKEAEKMER-ARHSYVLPLLGVCVERRSLGLVMEYMENGS- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREA--SRVVRDVAAALDFLH--TKGIAHRDLKPENILCESPEKvspVKICDFDLGS--GMKLNNSCTP 194
Cdd:cd13978    79 LKSLLEREIQDVPWSlrFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFH---VKISDFGLSKlgMKSISANRRR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPELTTPCgsaeYMAPEVVEVFTDQATfydKRCDLWSLGVVLYIMLSGYPPFVG-------HCGADCGwDR---GEVC 264
Cdd:cd13978   156 GTENLGGTPI----YMAPEAFDDFNKKPT---SKSDVYSFAIVIWAVLTRKEPFENainplliMQIVSKG-DRpslDDIG 227

                  ....*.
gi 1358101401 265 RVCQNK 270
Cdd:cd13978   228 RLKQIE 233
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
43-321 2.89e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 88.26  E-value: 2.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQ-GNKNILELIEFFEDDTRF-YLVFEKLQGGSI 120
Cdd:cd08223     8 IGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKlKHPNIVSYKESFEGEDGFlYIVMGFCEGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICdfDLGSGMKLNNSCTpittp 198
Cdd:cd08223    88 YTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL---TKSNIIKVG--DLGIARVLESSSD----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTPCGSAEYMAPevvEVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHcgadcgwdrgevcrvCQNKLFESIQEG 278
Cdd:cd08223   158 MATTLIGTPYYMSP---ELFSNKP--YNHKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYKILEG 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1358101401 279 KYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd08223   218 KLPPMPKQY---SPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
43-321 2.98e-20

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 90.09  E-value: 2.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVeTLYQCQGNKNILELIEFF------EDDTRFYLVFEK 114
Cdd:cd07876    29 IGSGAQGIVCAAFDTVLGINVAVKKLSRpfQNQTHAKRAYREL-VLLKCVNHKNIISLLNVFtpqkslEEFQDVYLVMEL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGsiLAHIQKQKHFNEReASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNNSCTP 194
Cdd:cd07876   108 MDAN--LCQVIHMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDFGLARTACTNFMMTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTpelttpcgSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcGWDR-----GEVCRVCQN 269
Cdd:cd07876   182 YVV--------TRYYRAPEVI-----LGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHID-QWNKvieqlGTPSAEFMN 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 270 KLFESIQ---EGKYEFPD-------KDWAHIS---------SEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07876   248 RLQPTVRnyvENRPQYPGisfeelfPDWIFPSeserdklktSQARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
43-321 8.17e-20

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 88.95  E-value: 8.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVeTLYQCQGNKNILELIEFF------EDDTRFYLVFEk 114
Cdd:cd07875    32 IGSGAQGIVCAAYDAILERNVAIKKLSRpfQNQTHAKRAYREL-VLMKCVNHKNIIGLLNVFtpqkslEEFQDVYIVME- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTP 194
Cdd:cd07875   110 LMDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDF----GLARTAGTSF 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPELTTpcgsAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcGWDR-----GEVCRVCQN 269
Cdd:cd07875   181 MMTPYVVT----RYYRAPEVI-----LGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHID-QWNKvieqlGTPCPEFMK 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 270 KLFESIQ-----EGKYE-------FPD----KDWAH---ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07875   251 KLQPTVRtyvenRPKYAgysfeklFPDvlfpADSEHnklKASQARDLLSKMLVIDASKRISVDEALQHPYI 321
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
41-324 8.74e-20

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 87.85  E-value: 8.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEkQAGHSRSRVFREVETLYQCQGNKNILELIEFFED------DTRFYLVFEK 114
Cdd:cd06637    12 ELVGNGTYGQVYKGRHVKTGQLAAIKVMD-VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKknppgmDDQLWLVMEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK--HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFdlGSGMKLNNs 191
Cdd:cd06637    91 CGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLlTENAE----VKLVDF--GVSAQLDR- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpiTTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgwdrgeVCRVCQNK- 270
Cdd:cd06637   164 ----TVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPP---------------LCDMHPMRa 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 271 LFESIQEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd06637   225 LFLIPRNPAPRLKSKKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQ 275
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
94-321 1.06e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 87.09  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  94 NILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRD----VAAALDFLHTKGIAHRDLKPENILCesp 169
Cdd:cd08222    63 AIVKFHDSFVEKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDwfiqLLLAVQYMHERRILHRDLKAKNIFL--- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 170 eKVSPVKICDFdlGSGMKLNNSCTpittpELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYimlsgyppfv 249
Cdd:cd08222   140 -KNNVIKVGDF--GISRILMGTSD-----LATTFTGTPYYMSPEVL-----KHEGYNSKSDIWSLGCILY---------- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 250 ghcgadcgwdrgEVCrvCQNKLFE---------SIQEGKY-EFPDKDwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08222   197 ------------EMC--CLKHAFDgqnllsvmyKIVEGETpSLPDKY----SKELNAIYSRMLNKDPALRPSAAEILKIP 258

                  ..
gi 1358101401 320 WV 321
Cdd:cd08222   259 FI 260
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
59-319 1.45e-19

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 86.56  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  59 NGKEYAVKIIEKQaghSRSRVFREVETLYQCQGNKNIlelIEFF--EDDTRF-YLVFEKLQggSILAHIQKQKH------ 129
Cdd:cd13982    24 DGRPVAVKRLLPE---FFDFADREVQLLRESDEHPNV---IRYFctEKDRQFlYIALELCA--ASLQDLVESPResklfl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 130 FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVK--ICDFDLGSGMKLNNSctpiTTPELTTPCGSA 207
Cdd:cd13982    96 RPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRamISDFGLCKKLDVGRS----SFSRRSGVAGTS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 208 EYMAPEV-VEVFTDQATfydKRCDLWSLGVVLYIMLS-GYPPFVGHCGADCGWDRGEVCRVCQNKLfesiqegkyefpdk 285
Cdd:cd13982   172 GWIAPEMlSGSTKRRQT---RAVDIFSLGCVFYYVLSgGSHPFGDKLEREANILKGKYSLDKLLSL-------------- 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1358101401 286 dwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd13982   235 --GEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
41-320 1.63e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 86.70  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd07861     6 EKIGEGTYGVVYKGRNKKTGQIVAMKKIrlESEEEGVPSTAIREISLLKELQ-HPNIVCLEDVLMQENRLYLVFEFLSMD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 --SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLnnsctPIT 196
Cdd:cd07861    85 lkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADFGLARAFGI-----PVR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 --TPELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLF-- 272
Cdd:cd07861   157 vyTHEVVT----LWYRAPEVLL----GSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWpg 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 273 -ESIQEGKYEFPdkDWA---------HISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07861   229 vTSLPDYKNTFP--KWKkgslrtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
42-323 1.82e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 86.86  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEK---------QAGHSRSRVFREVETLYqcqgnknILELIEFFEDDTRFYLVF 112
Cdd:cd05608     8 VLGKGGFGEVSACQMRATGKLYACKKLNKkrlkkrkgyEGAMVEKRILAKVHSRF-------IVSLAYAFQTKTDLCLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHI----QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKL 188
Cdd:cd05608    81 TIMNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD---GNVRISDLGLAVELKD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNSCTpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdRGEvcRVCQ 268
Cdd:cd05608   158 GQTKT-------KGYAGTPGFMAPELL-----LGEEYDYSVDYFTLGVTLYEMIAARGPFRA---------RGE--KVEN 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 269 NKLFESIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG 323
Cdd:cd05608   215 KELKQRILNDSVTYSEK----FSPASKSICEALLAKDPEKRLgfrdgNCDGLRTHPFFRD 270
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
40-250 2.51e-19

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 85.66  E-value: 2.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   40 SELLGEGAYAKV-QGAVSLQNGKEY---AVKIIekQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:smart00219   4 GKKLGEGAFGEVyKGKLKGKGGKKKvevAVKTL--KEDASeqqIEEFLREARIMRKLD-HPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  113 EKLQGGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDF----DLGSG-- 185
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFglsrDLYDDdy 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401  186 MKLNNSCTPITtpelttpcgsaeYMAPEVVE--VFTdqatfydKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:smart00219 158 YRKRGGKLPIR------------WMAPESLKegKFT-------SKSDVWSFGVLLWEIFTlGEQPYPG 206
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
43-320 3.33e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 86.17  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR---SRVfREVETLYQCQG--NKNILELIEF-----FEDDTRFYLVF 112
Cdd:cd07863     8 IGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGlplSTV-REVALLKRLEAfdHPNIVRLMDVcatsrTDRETKVTLVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGgSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlgsGMKLNN 190
Cdd:cd07863    87 EHVDQ-DLRTYLDKvpPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQ---VKLADF----GLARIY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCTPITTPELTTpcgsAEYMAPEVVEvftdQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRV---- 266
Cdd:cd07863   159 SCQMALTPVVVT----LWYRAPEVLL----QST-YATPVDMWSVGCIFAEMFRRKPLFCGNSEAD------QLGKIfdli 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 267 ---CQNKLFESIQEGKYEFP-------DKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07863   224 glpPEDDWPRDVTLPRGAFSprgprpvQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPF 287
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
31-323 3.68e-19

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 86.65  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAG--HSRSRVFREVETL-YQCQGN----KNILELIEFFE 103
Cdd:cd07855     2 DVGDRYEPI-ETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDvvTTAKRTLRELKILrHFKHDNiiaiRDILRPKVPYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFEKLQggSILAH-IQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKIC 178
Cdd:cd07855    81 DFKDVYVVLDLME--SDLHHiIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLvnenCE-------LKIG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFDLGSGMKLN--NSCTPITTPELTTPcgsaeYMAPEVVEVFTDqatfYDKRCDLWSLGVV------------------- 237
Cdd:cd07855   152 DFGMARGLCTSpeEHKYFMTEYVATRW-----YRAPELMLSLPE----YTQAIDMWSVGCIfaemlgrrqlfpgknyvhq 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 238 --LYIMLSGYPP--FVGHCGADcgwdrgevcRVcqNKLFESIQEGkyefPDKDWAHI----SSEAKDLISKLLVRDAKQR 309
Cdd:cd07855   223 lqLILTVLGTPSqaVINAIGAD---------RV--RRYIQNLPNK----QPVPWETLypkaDQQALDLLSQMLRFDPSER 287
                         330
                  ....*....|....
gi 1358101401 310 LSAAQVLQHPWVQG 323
Cdd:cd07855   288 ITVAEALQHPFLAK 301
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
41-322 4.94e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 85.52  E-value: 4.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQGNKNILELIEFF-----EDDTRFYLVFEK 114
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfDPESPETSKEVSALECEIQLLKNLQHERIVQYYgclrdRAEKTLTIFMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFdlGSGMKLNNSCTP 194
Cdd:cd06651    93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS---AGNVKLGDF--GASKRLQTICMS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPELTTpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVcrvcQNKLFE- 273
Cdd:cd06651   168 GTGIRSVT--GTPYWMSPEVI-----SGEGYGRKADVWSLGCTVVEMLTEKPP----------WAEYEA----MAAIFKi 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 274 SIQEGKYEFPdkdwAHISSEAKDLISKLLVrDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06651   227 ATQPTNPQLP----SHISEHARDFLGCIFV-EARHRPSAEELLRHPFAQ 270
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
38-321 5.39e-19

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 85.88  E-value: 5.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIE---------KQAGHSRS----RVFREVEtlyqcqgNKNILELIEFFED 104
Cdd:cd14041     9 LLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQlnknwrdekKENYHKHAcreyRIHKELD-------HPRIVKLYDYFSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DT-RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHT--KGIAHRDLKPENILCESPEKVSPVKICDFD 181
Cdd:cd14041    82 DTdSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTACGEIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSGMKlNNSCTPITTPELTTP-CGSAEYMAPEVVEVFTDQATFYDKrCDLWSLGVVLYIMLSGYPPFvghcgadcGWDR 260
Cdd:cd14041   162 LSKIMD-DDSYNSVDGMELTSQgAGTYWYLPPECFVVGKEPPKISNK-VDVWSVGVIFYQCLYGRKPF--------GHNQ 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 261 GEVCRVCQNKLFESIQegkYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14041   232 SQQDILQENTILKATE---VQFPPK--PVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
36-321 5.81e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 85.92  E-value: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGA--VSLQNGKEYAVKIIEKQAGHSRS--RVFREVETLYQCQGNKNILELIEF---FEDDTRF 108
Cdd:cd07857     2 YELIKEL-GQGAYGIVCSArnAETSEEETVAIKKITNVFSKKILakRALRELKLLRHFRGHKNITCLYDMdivFPGNFNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKL 188
Cdd:cd07857    81 LYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCE---LKICDFGLARGFSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNSctpITTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVG------------------ 250
Cdd:cd07857   158 NPG---ENAGFMTEYVATRWYRAPEIMLSFQS----YTKAIDVWSVGCILAELLGRKPVFKGkdyvdqlnqilqvlgtpd 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 251 -----HCGADCGWDRGEVCRVCQNKLFESIqegkyeFPDKdwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07857   231 eetlsRIGSPKAQNYIRSLPNIPKKPFESI------FPNA-----NPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
43-321 6.08e-19

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 85.29  E-value: 6.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR-SRVFREVETLYQCqgnkNILELIEF---FEDDTRFYLVFEKLQGG 118
Cdd:cd06622     9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKfNQIIMELDILHKA----VSPYIVDFygaFFIEGAVYMCMEYMDAG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SiLAHIQKQKHFNEREASRVVRDVAAA----LDFLHTK-GIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCT 193
Cdd:cd06622    85 S-LDKLYAGGVATEGIPEDVLRRITYAvvkgLKFLKEEhNIIHRDVKPTNVLVNGNGQ---VKLCDFGVSGNLVASLAKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PIttpelttpcGSAEYMAPEVVEVFT-DQATFYDKRCDLWSLGVVLYIMLSG---YPPfvghcgadcgwdrgEVCRVCQN 269
Cdd:cd06622   161 NI---------GCQSYMAPERIKSGGpNQNPTYTVQSDVWSLGLSILEMALGrypYPP--------------ETYANIFA 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 KLfESIQEGKyefPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06622   218 QL-SAIVDGD---PPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
43-320 6.33e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 86.60  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFR---EVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHvkaERDILAEAD-NEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKL----------- 188
Cdd:cd05626    88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLD---GHIKLTDFGLCTGFRWthnskyyqkgs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 ---NNSCTPITTPELTTPC--------------------------GSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLY 239
Cdd:cd05626   165 hirQDSMEPSDLWDDVSNCrcgdrlktleqratkqhqrclahslvGTPNYIAPEVL-----LRKGYTQLCDWWSVGVILF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 240 IMLSGYPPFVGHCGADcgwdrgevcrvCQNKLFEsiQEGKYEFPDKdwAHISSEAKDLISKLLVrDAKQRL---SAAQVL 316
Cdd:cd05626   240 EMLVGQPPFLAPTPTE-----------TQLKVIN--WENTLHIPPQ--VKLSPEAVDLITKLCC-SAEERLgrnGADDIK 303

                  ....
gi 1358101401 317 QHPW 320
Cdd:cd05626   304 AHPF 307
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
43-323 6.57e-19

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 86.34  E-value: 6.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVETLYQCQgNKNILELIE--------FFEDdtrFYLVF 112
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMPNvfQNLVSCKRVFRELKMLCFFK-HDNVLSALDilqpphidPFEE---IYVVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQggSILaH--IQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNN 190
Cdd:cd07853    84 ELMQ--SDL-HkiIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSN---CVLKICDFGLARVEEPDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCtpITTPELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPF------------VGHCGADCGW 258
Cdd:cd07853   158 SK--HMTQEVVT----QYYRAPEILM----GSRHYTSAVDIWSVGCIFAELLGRRILFqaqspiqqldliTDLLGTPSLE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 259 DRGEVCRVCQNKLFESiqegKYEFPDKDW-----AHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd07853   228 AMRSACEGARAHILRG----PHKPPSLPVlytlsSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
43-323 7.42e-19

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 85.18  E-value: 7.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS-RSRVFREVETLYQCQgNKNILELI-EFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSvRKQILRELQILHECH-SPYIVSFYgAFLNENNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSCTpittpe 199
Cdd:cd06620    92 DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQ---IKLCDF--GVSGELINSIA------ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 lTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRgevcrvcQNKLFESIQ--- 276
Cdd:cd06620   161 -DTFVGTSTYMSPERI-----QGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNG-------PMGILDLLQriv 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 277 -EGKYEFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd06620   228 nEPPPRLPKDR--IFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
42-327 7.78e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 85.88  E-value: 7.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-----AGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05633    12 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCES--PEKVSPVKI-CDFdlgSGMKLNNSct 193
Cdd:cd05633    92 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEhgHVRISDLGLaCDF---SKKKPHAS-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pittpelttpCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwDRGEVCRVCQNKlfe 273
Cdd:cd05633   167 ----------VGTHGYMAPEVLQ----KGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK----DKHEIDRMTLTV--- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 274 siqegKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQG-EQQH 327
Cdd:cd05633   226 -----NVELPDS----FSPELKSLLEGLLQRDVSKRLgchgrGAQEVKEHSFFKGiDWQQ 276
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
31-320 7.93e-19

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 85.12  E-value: 7.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVK---------IIEKQAghsrsrvFREVETLYQCQgNKNILELIEF 101
Cdd:cd07847     2 KYEKLSKI-----GEGSYGVVFKCRNRETGQIVAIKkfveseddpVIKKIA-------LREIRMLKQLK-HPNLVNLIEV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 102 FEDDTRFYLVFEKLQGgSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDF 180
Cdd:cd07847    69 FRRKRKLHLVFEYCDH-TVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILI---TKQGQIKLCDF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 dlGSGMKLNNSCTpittpELTTPCGSAEYMAPEVveVFTDqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGW-- 258
Cdd:cd07847   145 --GFARILTGPGD-----DYTDYVATRWYRAPEL--LVGD--TQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYli 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 259 --DRGEVCR-----VCQNKLFESIQ----EGKYEFPDKdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07847   214 rkTLGDLIPrhqqiFSTNQFFKGLSipepETREPLESK-FPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
41-321 1.03e-18

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 84.67  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCQGNKNILELIEFF------EDDTRFYLVFEK 114
Cdd:cd06636    22 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE-DEEEEIKLEINMLKKYSHHRNIATYYGAFikksppGHDDQLWLVMEF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK--HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-CESPEkvspVKICDFdlGSGMKLNNs 191
Cdd:cd06636   101 CGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLlTENAE----VKLVDF--GVSAQLDR- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 ctpiTTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgwdrgeVCRVCQNK- 270
Cdd:cd06636   174 ----TVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP---------------LCDMHPMRa 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFESIQEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06636   235 LFLIPRNPPPKLKSKKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
43-248 1.13e-18

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 85.24  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSR--VFREVETLYQCQgNKNILELIEFFEDDTRFY--LVFEKLQGG 118
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVF-NNLSFMRPLdvQMREFEVLKKLN-HKNIVKLFAIEEELTTRHkvLVMELCPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 S---ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPV-KICDFdlGSGMKLNNSctp 194
Cdd:cd13988    79 SlytVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDF--GAARELEDD--- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 195 ittPELTTPCGSAEYMAPEVVE---VFTDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd13988   154 ---EQFVSLYGTEEYLHPDMYEravLRKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
43-321 1.13e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 85.53  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVeTLYQCQGNKNILELIEFF------EDDTRFYLVFEk 114
Cdd:cd07874    25 IGSGAQGIVCAAYDAVLDRNVAIKKLSRpfQNQTHAKRAYREL-VLMKCVNHKNIISLLNVFtpqkslEEFQDVYLVME- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCTP 194
Cdd:cd07874   103 LMDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDF----GLARTAGTSF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPELTTpcgsAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcGWDR-----GEVCRVCQN 269
Cdd:cd07874   174 MMTPYVVT----RYYRAPEVI-----LGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYID-QWNKvieqlGTPCPEFMK 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 270 KLFESIQ-----EGKYE-------FPDK----DWAH---ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07874   244 KLQPTVRnyvenRPKYAgltfpklFPDSlfpaDSEHnklKASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
41-318 1.24e-18

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 84.13  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGKEY--AVKIIEKQAGHS-RSRVFREVETLYQCqGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd00192     1 KKLGEGAFGEVyKGKLKGGDGKTVdvAVKTLKEDASESeRKDFLKEARVMKKL-GHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVV---------RDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDF---- 180
Cdd:cd00192    80 GGDLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCL------VGEdlvVKISDFglsr 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 ---DLGSGMKLNNSCTPIttpelttpcgsaEYMAPEVVE--VFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVGhcga 254
Cdd:cd00192   154 diyDDDYYRKKTGGKLPI------------RWMAPESLKdgIFTSKS-------DVWSFGVLLWeIFTLGATPYPG---- 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 255 dcgwdrgevcrvCQNK-LFESIQEGKY-EFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd00192   211 ------------LSNEeVLEYLRKGYRlPKPE----NCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
41-331 1.39e-18

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 85.05  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS-RVFREVETL--YQCQGNKNILELI-----EFFEDdtrFYLVF 112
Cdd:cd07849    11 SYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYClRTLREIKILlrFKHENIIGILDIQrpptfESFKD---VYIVQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQggSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGSgmkl 188
Cdd:cd07849    88 ELME--TDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLlntnCD-------LKICDFGLAR---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 nnsctpITTPE------LTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVG--------HCGA 254
Cdd:cd07849   155 ------IADPEhdhtgfLTEYVATRWYRAPEIMLNSKG----YTKAIDIWSVGCILAEMLSNRPLFPGkdylhqlnLILG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 255 DCGWDRGE-VCRVCQNKLFESIQegkyEFPDKD---WA----HISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVqgEQQ 326
Cdd:cd07849   225 ILGTPSQEdLNCIISLKARNYIK----SLPFKPkvpWNklfpNADPKALDLLDKMLTFNPHKRITVEEALAHPYL--EQY 298

                  ....*
gi 1358101401 327 HNGPD 331
Cdd:cd07849   299 HDPSD 303
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
61-320 1.73e-18

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 83.75  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  61 KEYAVKIIEKQAghsrsrvFREVETL--YQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRV 138
Cdd:PHA03390   42 KLFVQKIIKAKN-------FNAIEPMvhQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 139 VRDVAAALDFLHTKGIAHRDLKPENILCESPEKvsPVKICDFDLgsgmklnnsCTPITTPelTTPCGSAEYMAPEVVEVF 218
Cdd:PHA03390  115 IRQLVEALNDLHKHNIIHNDIKLENVLYDRAKD--RIYLCDYGL---------CKIIGTP--SCYDGTLDYFSPEKIKGH 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 219 TDQATFydkrcDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVcqNKLfESIQEGKYEFPdkdwAHISSEAKDLI 298
Cdd:PHA03390  182 NYDVSF-----DWWAVGVLTYELLTGKHPFKE--------DEDEELDL--ESL-LKRQQKKLPFI----KNVSKNANDFV 241
                         250       260
                  ....*....|....*....|...
gi 1358101401 299 SKLLVRDAKQRLSA-AQVLQHPW 320
Cdd:PHA03390  242 QSMLKYNINYRLTNyNEIIKHPF 264
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
43-321 2.19e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 84.39  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEK--QAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRF------YLVFEk 114
Cdd:cd07850     8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRpfQNVTHAKRAYREL-VLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLVME- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQ-KHfnEReASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKLNNSCT 193
Cdd:cd07850    86 LMDANLCQVIQMDlDH--ER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILDF----GLARTAGTS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 PITTPELTTpcgsAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcGWDR-----GEVCRVCQ 268
Cdd:cd07850   156 FMMTPYVVT----RYYRAPEVI-----LGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHID-QWNKiieqlGTPSDEFM 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 269 NKLFESI-----QEGKYE-------FPD-------KDWAHI-SSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07850   226 SRLQPTVrnyveNRPKYAgysfeelFPDvlfppdsEEHNKLkASQARDLLSKMLVIDPEKRISVDDALQHPYI 298
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
41-250 3.02e-18

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 82.98  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   41 ELLGEGAYAKVQGAVSLQNGKEY----AVKIIEKQAGHS-RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:smart00221   5 KKLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDASEQqIEEFLREARIMRKLD-HPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  116 QGGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDF----DLGSG--MK 187
Cdd:smart00221  84 PGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFglsrDLYDDdyYK 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401  188 LNNSCTPITtpelttpcgsaeYMAPEVVE--VFTdqatfydKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:smart00221 161 VKGGKLPIR------------WMAPESLKegKFT-------SKSDVWSFGVLLWEIFTlGEEPYPG 207
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
41-238 3.86e-18

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 82.85  E-value: 3.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQ-NGKEYAVKIIEKQAG--HSRSRVFREVETL--YQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14052     6 ELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAgaKDRLRRLEEVSILreLTLDGHDNIVQLIDSWEYHGHLYIQTELC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSI---LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlgsGMKlnNSC 192
Cdd:cd14052    86 ENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFE---GTLKIGDF----GMA--TVW 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 193 TPITTPELTtpcGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVL 238
Cdd:cd14052   157 PLIRGIERE---GDREYIAPEILSEHM-----YDKPADIFSLGLIL 194
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
30-320 4.69e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 83.13  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDmYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKII----EKQAGHSRSrvFREVETLYQCQgNKNILELIEFF--- 102
Cdd:cd07866     5 SKLRD-YEIL-GKLGEGTFGEVYKARQIKTGRVVALKKIlmhnEKDGFPITA--LREIKILKKLK-HPNVVPLIDMAver 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 ---EDDTR--FYLVF----EKLQGgsiLAHIQKQkHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvS 173
Cdd:cd07866    80 pdkSKRKRgsVYMVTpymdHDLSG---LLENPSV-KLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQ---G 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 174 PVKICDFDL-----GSGMKLNNSCTPiTTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd07866   153 ILKIADFGLarpydGPPPNPKGGGGG-GTRKYTNLVVTRWYRPPELLL----GERRYTTAVDIWGIGCVFAEMFTRRPIL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 249 VGHCGAD--------CG------WDRGEVCRVCQNKLFESIQEGKYEfpdKDWAHISSEAKDLISKLLVRDAKQRLSAAQ 314
Cdd:cd07866   228 QGKSDIDqlhlifklCGtpteetWPGWRSLPGCEGVHSFTNYPRTLE---ERFGKLGPEGLDLLSKLLSLDPYKRLTASD 304

                  ....*.
gi 1358101401 315 VLQHPW 320
Cdd:cd07866   305 ALEHPY 310
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
40-318 5.16e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 82.36  E-value: 5.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghsrsrvFREVETLYQ-CQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd13995     9 SDFIPRGAFGKVYLAQDTKTKKRMACKLIPVEQ-------FKPSDVEIQaCFRHENIAELYGALLWEETVHLFMEAGEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvkICDFDLGSGMKLNnsctpITTP 198
Cdd:cd13995    82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV----LVDFGLSVQMTED-----VYVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 ELTTpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrGEVCRVCQNKLFESIQeg 278
Cdd:cd13995   153 KDLR--GTEIYMSPEVI-----LCRGHNTKADIYSLGATIIHMQTGSPPWV-----------RRYPRSAYPSYLYIIH-- 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 279 KYEFPDKDWAHISSEA-KDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd13995   213 KQAPPLEDIAQDCSPAmRELLEAALERNPNHRSSAAELLKH 253
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
41-322 5.87e-18

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 82.73  E-value: 5.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaghsrSRVFREVETLYqcqgnkNILELIEFFEDDTRFY----------- 109
Cdd:cd06639    28 ETIGKGTYGKVYKVTNKKDGSLAAVKILDPI-----SDVDEEIEAEY------NILRSLPNHPNVVKFYgmfykadqyvg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 ----LVFEKLQGGSILAHIQ----KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFD 181
Cdd:cd06639    97 gqlwLVLELCNGGSVTELVKgllkCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSgmklnnsctPITTPEL--TTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWD 259
Cdd:cd06639   174 VSA---------QLTSARLrrNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPL---------FD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 260 RGEVcrvcqNKLFESIQEGKYEF--PDKdWAHissEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06639   236 MHPV-----KALFKIPRNPPPTLlnPEK-WCR---GFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
41-247 6.09e-18

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 82.43  E-value: 6.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd06641    10 EKIGKGSFGEVFKGIDNRTQKVVAIKIIDlEEAEDEIEDIQQEITVLSQCD-SPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNsctpiTTPE 199
Cdd:cd06641    89 ALDLLEPGP-LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE---VKLADF--GVAGQLTD-----TQIK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPP 247
Cdd:cd06641   158 RN*FVGTPFWMAPEVI-----KQSAYDSKADIWSLGITAIELARGEPP 200
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
31-320 6.31e-18

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 83.11  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSelLGEGAYAKVQGAvSLQNGKEYAV--------KII-EKQAGHsrsrVFREVETLYQCQgNKNILELIEF 101
Cdd:PTZ00426   28 KYEDFNFIRT--LGTGSFGRVILA-TYKNEDFPPVaikrfeksKIIkQKQVDH----VFSERKILNYIN-HPFCVNLYGS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 102 FEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFD 181
Cdd:PTZ00426  100 FKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL---DKDGFIKMTDFG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSgmklnnsctpITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrg 261
Cdd:PTZ00426  177 FAK----------VVDTRTYTLCGTPEYIAPEIL-----LNVGHGKAADWWTLGIFIYEILVGCPPFYANEPL------- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 262 evcrvcqnKLFESIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPW 320
Cdd:PTZ00426  235 --------LIYQKILEGIIYFPK----FLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPW 286
PTZ00284 PTZ00284
protein kinase; Provisional
36-331 6.44e-18

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 84.25  E-value: 6.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSeLLGEGAYAKVQGAVSLQNgKEY-AVKIIEKQAGHSRSR----VFREVETLYQCQGNKNILELIEFFEDDTRFYL 110
Cdd:PTZ00284  131 FKILS-LLGEGTFGKVVEAWDRKR-KEYcAVKIVRNVPKYTRDAkieiQFMEKVRQADPADRFPLMKIQRYFQNETGHMC 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEK-VSP------------VK 176
Cdd:PTZ00284  209 IVMPKYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDTvVDPvtnralppdpcrVR 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 177 ICdfDLGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVevfTDQATFYDKrcDLWSLGVVLYIMLSGYPPFVGH----- 251
Cdd:PTZ00284  289 IC--DLGGCCDERHSRTAIVS--------TRHYRSPEVV---LGLGWMYST--DMWSMGCIIYELYTGKLLYDTHdnleh 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 252 --------------CGADCGWDRGEVcrvcqnkLFESIQEGKyefPDKDWAHISSEAK--------------DLISKLLV 303
Cdd:PTZ00284  354 lhlmektlgrlpseWAGRCGTEEARL-------LYNSAGQLR---PCTDPKHLARIARarpvrevirddllcDLIYGLLH 423
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1358101401 304 RDAKQRLSAAQVLQHPWV-----QGEQQHNGPD 331
Cdd:PTZ00284  424 YDRQKRLNARQMTTHPYVlkyypECRQHPNYPD 456
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
41-319 7.81e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 81.71  E-value: 7.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQ------CQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQV-SFCRNSSSEQEEVVEAIREeirmmaRLNHPNIVRMLGATQHKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFdlGSGMKLNNSCTp 194
Cdd:cd06630    85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR--LRIADF--GAAARLASKGT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 iTTPELTTP-CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVcrvcQNKL-- 271
Cdd:cd06630   160 -GAGEFQGQlLGTIAFMAPEVL-----RGEQYGRSCDVWSVGCVIIEMATAKPP----------WNAEKI----SNHLal 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 -FE-SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd06630   220 iFKiASATTPPPIPE----HLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
44-320 1.30e-17

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 81.95  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  44 GEGAYAKVQGAVSLQN--GKEYAVKIIE----KQAGHSRSRVfREVETLYQCQgNKNILELIEFF--EDDTRFYLVFEKL 115
Cdd:cd07842     9 GRGTYGRVYKAKRKNGkdGKEYAIKKFKgdkeQYTGISQSAC-REIALLRELK-HENVVSLVEVFleHADKSVYLLFDYA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 Q---GGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC--ESPEKVSpVKICDFDLGsgmKLN 189
Cdd:cd07842    87 EhdlWQIIKFHRQAKRVsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgEGPERGV-VKIGDLGLA---RLF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSctPITTP-ELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHCGAD-----CGWDRGEV 263
Cdd:cd07842   163 NA--PLKPLaDLDPVVVTIWYRAPELLL----GARHYTKAIDIWAIGCIFAELLTLEPIF--KGREAkikksNPFQRDQL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 264 CRVCQ-------------------NKLFESIQEGKYEFPDK-DWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd07842   235 ERIFEvlgtptekdwpdikkmpeyDTLKSDTKASTYPNSLLaKWMHKhkkpDSQGFDLLRKLLEYDPTKRITAEEALEHP 314

                  .
gi 1358101401 320 W 320
Cdd:cd07842   315 Y 315
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
41-320 1.72e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 81.37  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGH-SRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGgS 119
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEgTPSTAIREISLMKELK-HENIVRLHDVIHTENKLMLVFEYMDK-D 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRV---VRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLnnsctPIT 196
Cdd:cd07836    84 LKKYMDTHGVRGALDPNTVksfTYQLLKGIAFCHENRVLHRDLKPQNLLI---NKRGELKLADFGLARAFGI-----PVN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 T--PELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwDRGEVCRVC------- 267
Cdd:cd07836   156 TfsNEVVT----LWYRAPDVLL----GSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNED---QLLKIFRIMgtptest 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 268 --QNKLFESIQEGKYEFPDKDWA----HISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07836   225 wpGISQLPEYKPTFPRYPPQDLQqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
33-321 1.75e-17

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 80.73  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVF 112
Cdd:cd14110     2 EKTYAFQTEI-NRGRFSVVRQCEEKRSGQMLAAKIIPYKP-EDKQLVLREYQVLRRLS-HPRIAQLHSAYLSPRHLVLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVkicdfDLGSGMKLNNSC 192
Cdd:cd14110    79 ELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIV-----DLGNAQPFNQGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPIttpelTTPCGS-AEYMAPEVVEvftDQATFydKRCDLWSLGVVLYIMLSGYPPFvghcGADCGWDRgevcrvcqnkl 271
Cdd:cd14110   154 VLM-----TDKKGDyVETMAPELLE---GQGAG--PQTDIWAIGVTAFIMLSADYPV----SSDLNWER----------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 272 FESIQEGKYEFpDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14110   209 DRNIRKGKVQL-SRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
38-321 2.76e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 80.87  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIE---------KQAGHSRS----RVFREVEtlyqcqgNKNILELIEFFED 104
Cdd:cd14040     9 LLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQlnkswrdekKENYHKHAcreyRIHKELD-------HPRIVKLYDYFSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DT-RFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLH--TKGIAHRDLKPENILCESPEKVSPVKICDFD 181
Cdd:cd14040    82 DTdTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSGMklNNSCTPITTPELTTP-CGSAEYMAPEVVEVFTDQATFYDKrCDLWSLGVVLYIMLSGYPPFvghcgadcGWDR 260
Cdd:cd14040   162 LSKIM--DDDSYGVDGMDLTSQgAGTYWYLPPECFVVGKEPPKISNK-VDVWSVGVIFFQCLYGRKPF--------GHNQ 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 261 GEVCRVCQNKLFESIQegkYEFPDKdwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14040   231 SQQDILQENTILKATE---VQFPVK--PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
41-321 2.79e-17

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 80.45  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRvfREVETLyQCQ-------GNKNILELIEFFEDDT--RFYLV 111
Cdd:cd06653     8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETS--KEVNAL-ECEiqllknlRHDRIVQYYGCLRDPEekKLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFdlGSGMKLNNS 191
Cdd:cd06653    85 VEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDS---AGNVKLGDF--GASKRIQTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 192 CTPITTPELTTpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVcrvcQNKL 271
Cdd:cd06653   160 CMSGTGIKSVT--GTPYWMSPEVI-----SGEGYGRKADVWSVACTVVEMLTEKPP----------WAEYEA----MAAI 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 272 FE-SIQEGKYEFPDkdwaHISSEAKDLISKLLVRDaKQRLSAAQVLQHPWV 321
Cdd:cd06653   219 FKiATQPTKPQLPD----GVSDACRDFLRQIFVEE-KRRPTAEFLLRHPFV 264
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
41-322 5.50e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 79.73  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEK-QAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLqgGS 119
Cdd:cd06618    21 GEIGSGTCGQVYKMRHKKTGHVMAVKQMRRsGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELM--ST 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQK--QKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCEspeKVSPVKICDFDLgSGmKLNNSCTPit 196
Cdd:cd06618    99 CLDKLLKriQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLD---ESGNVKLCDFGI-SG-RLVDSKAK-- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpelTTPCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadCGWDRGEVCRVCQNKLFESIQ 276
Cdd:cd06618   172 ----TRSAGCAAYMAPERIDP--PDNPKYDIRADVWSLGISLVELATGQFPYRN-----CKTEFEVLTKILNEEPPSLPP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 277 EGKYefpdkdwahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06618   241 NEGF----------SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
43-321 5.77e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 79.85  E-value: 5.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKII----EKQaGHSRSRVfREVETLYQCQgNKNILEL----------IEFFEDDTRF 108
Cdd:cd07864    15 IGEGTYGQVYKAKDKDTGELVALKKVrldnEKE-GFPITAI-REIKILRQLN-HRSVVNLkeivtdkqdaLDFKKDKGAF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGsgmKL 188
Cdd:cd07864    92 YLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ---IKLADFGLA---RL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 NNS--CTPITTPELTTpcgsaEYMAPEVveVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGH------------CGA 254
Cdd:cd07864   166 YNSeeSRPYTNKVITL-----WYRPPEL--LLGEER--YGPAIDVWSCGCILGELFTKKPIFQANqelaqlelisrlCGS 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 255 DCGWDRGEVCRVcqnKLFESIQEGKY--EFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07864   237 PCPAVWPDVIKL---PYFNTMKPKKQyrRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
41-318 6.27e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 79.46  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEkqagHSRSRVFREVETLYQCQgNKNILELIEFFEDD--------------- 105
Cdd:cd14047    12 ELIGSGGFGQVFKAKHRIDGKTYAIKRVK----LNNEKAEREVKALAKLD-HPNIVRYNGCWDGFdydpetsssnssrsk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 106 -TRFYLVFEKLQGGSILAHIQKQ-KHFNER-EASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDL 182
Cdd:cd14047    87 tKCLFIQMEFCEKGTLESWIEKRnGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK---VKIGDFGL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLNNsctpittpELTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYppfvghcgaDCGWDRge 262
Cdd:cd14047   164 VTSLKNDG--------KRTKSKGTLSYMSPEQISSQD-----YGKEVDIYALGLILFELLHVC---------DSAFEK-- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 263 vcrvcqNKLFESIQEGkyEFPDKDWAHISSEAKdLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14047   220 ------SKFWTDLRNG--ILPDIFDKRYKIEKT-IIKKMLSKKPEDRPNASEILRT 266
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
30-320 7.03e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 79.72  E-value: 7.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKII----EKQAghsrsrvF-----REVETLyQCQGNKNILELIE 100
Cdd:cd07865    12 SKYEKLAKI-----GQGTFGEVFKARHRKTGQIVALKKVlmenEKEG-------FpitalREIKIL-QLLKHENVVNLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 101 --------FFEDDTRFYLVFE----KLQGgsILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCes 168
Cdd:cd07865    79 icrtkatpYNRYKGSIYLVFEfcehDLAG--LLSNKNVK--FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 169 pEKVSPVKICDFDLGSGMKLNNSCTPittPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd07865   153 -TKDGVLKLADFGLARAFSLAKNSQP---NRYTNRVVTLWYRPPELLLGERD----YGPPIDMWGAGCIMAEMWTRSPIM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 249 VGHCGAD--------CGWDRGEVCRVCQN-KLFESI---QEGKYEFPDKDWAHISS-EAKDLISKLLVRDAKQRLSAAQV 315
Cdd:cd07865   225 QGNTEQHqltlisqlCGSITPEVWPGVDKlELFKKMelpQGQKRKVKERLKPYVKDpYALDLIDKLLVLDPAKRIDADTA 304

                  ....*
gi 1358101401 316 LQHPW 320
Cdd:cd07865   305 LNHDF 309
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
43-321 7.13e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 79.30  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd06646    17 VGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECK-HCNIVAYFGSYLSREKLWICMEYCGGGSLQD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNnsctpITTPELTT 202
Cdd:cd06646    96 IYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADF--GVAAKIT-----ATIAKRKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPP-FVGHcgadcgwdrgevcrvCQNKLFeSIQEGKYE 281
Cdd:cd06646   166 FIGTPYWMAPEVAAV--EKNGGYNQLCDIWAVGITAIELAELQPPmFDLH---------------PMRALF-LMSKSNFQ 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 282 FPD-KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06646   228 PPKlKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
124-322 7.27e-17

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 79.39  E-value: 7.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 124 IQKQKHFNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCEspeKVSPVKICDFDLgSGmKLNNSCTPittpelTT 202
Cdd:cd06617    94 YDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLIN---RNGQVKLCDFGI-SG-YLVDSVAK------TI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVEVFTDQATfYDKRCDLWSLGVVLYIMLSG-YP------PFvghcgadcgwdrgevcrvcqNKLFESI 275
Cdd:cd06617   163 DAGCKPYMAPERINPELNQKG-YDVKSDVWSLGITMIELATGrFPydswktPF--------------------QQLKQVV 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 276 QEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06617   222 EEPSPQLPAEKF---SPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
41-323 7.49e-17

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 80.21  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGH--SRSRVFREVeTLYQCQGNKNILELIEF--------FEDdtrFYL 110
Cdd:cd07859     6 EVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHvsDATRILREI-KLLRLLRHPDIVEIKHImlppsrreFKD---IYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQggSILAHIQKQKHFNEREASRV-VRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMkLN 189
Cdd:cd07859    82 VFELME--SDLHQVIKANDDLTPEHHQFfLYQLLRALKYIHTANVFHRDLKPKNILANADCK---LKICDFGLARVA-FN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTPITtpeLTTPCGSAEYMAPEVVEVFTDQatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRG 261
Cdd:cd07859   156 DTPTAIF---WTDYVATRWYRAPELCGSFFSK---YTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHqldlitdlLGTPSP 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 262 EVCRVCQN---KLFESIQEGKYEFP-DKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQG 323
Cdd:cd07859   230 ETISRVRNekaRRYLSSMRKKQPVPfSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKG 295
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
43-331 1.05e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 79.28  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVfREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ---- 116
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDNLVALKEIrlEHEEGAPCTAI-REVSLLKDLK-HANIVTLHDIIHTEKSLTLVFEYLDkdlk 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 ------GGSILAHIQKQKHFnereasRVVRdvaaALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGmklnn 190
Cdd:cd07873    88 qylddcGNSINMHNVKLFLF------QLLR----GLAYCHRRKVLHRDLKPQNLLINERGE---LKLADFGLARA----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 scTPITTPELTTPCGSAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--------CGWDRGE 262
Cdd:cd07873   150 --KSIPTKTYSNEVVTLWYRPPDILLGSTD----YSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEqlhfifriLGTPTEE 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 263 VCR-VCQNKLFESIQEGKYeFPDKDWAH---ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ--GEQQHNGPD 331
Cdd:cd07873   224 TWPgILSNEEFKSYNYPKY-RADALHNHaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHslGERIHKLPD 297
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
42-322 1.09e-16

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 79.32  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-----AGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14223     7 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNNSCTPIt 196
Cdd:cd14223    87 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEF---GHVRISDLGLACDFSKKKPHASV- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpelttpcGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwDRGEVCRVCQNKlfesiq 276
Cdd:cd14223   163 --------GTHGYMAPEVLQ----KGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK----DKHEIDRMTLTM------ 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 277 egKYEFPDKdwahISSEAKDLISKLLVRDAKQRL-----SAAQVLQHPWVQ 322
Cdd:cd14223   221 --AVELPDS----FSPELRSLLEGLLQRDVNRRLgcmgrGAQEVKEEPFFR 265
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
40-250 1.17e-16

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 78.58  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAvsLQNGKEYAVKIIEKQAGHSRSR--VFREVETLYQcqGNKNILEL--IEFFEDDTRFYLVFEKL 115
Cdd:cd13979     8 QEPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRqsFWAELNAARL--RHENIVRVlaAETGTDFASLGLIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILahiqkQKHFNER-------EASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFdlGSG 185
Cdd:cd13979    84 CGNGTL-----QQLIYEGseplplaHRILISLDIARALRFCHSHGIVHLDVKPANIL------ISEqgvCKLCDF--GCS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 186 MKLNNSCtpittpELTTPC----GSAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd13979   151 VKLGEGN------EVGTPRshigGTYTYRAPELLkgERVTPKA-------DIYSFGITLWQMLTRELPYAG 208
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
36-322 1.67e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 79.03  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELLGEGAYAKVQGAVSLQNGKEYA---VKIIEKQAGHSRSR-----------VFREVETLYQCQgNKNILELIEF 101
Cdd:PTZ00024   10 YIQKGAHLGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRqlvgmcgihftTLRELKIMNEIK-HENIMGLVDV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 102 FEDDTRFYLVFEKLQGGsiLAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspeKVSPVKICDF 180
Cdd:PTZ00024   89 YVEGDFINLVMDIMASD--LKKVVDRKiRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFIN---SKGICKIADF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 DLGSgmKLNNSCTPITTPELTTPCgSAEYMAPEVVEVFTDQ------ATFYDKRCDLWSLGVVLYIMLSGYPPFVGH--- 251
Cdd:PTZ00024  164 GLAR--RYGYPPYSDTLSKDETMQ-RREEMTSKVVTLWYRApellmgAEKYHFAVDMWSVGCIFAELLTGKPLFPGEnei 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 252 -----------CGADCGWDRGEVCRVCQNKLFESIQEGKYEFPdkdwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:PTZ00024  241 dqlgrifellgTPNEDNWPQAKKLPLYTEFTPRKPKDLKTIFP-----NASDDAIDLLQSLLKLNPLERISAKEALKHEY 315

                  ..
gi 1358101401 321 VQ 322
Cdd:PTZ00024  316 FK 317
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
34-319 2.03e-16

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 78.02  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS---------RVFREVETLYqcqgnknILELIEFFED 104
Cdd:cd05607     1 DKYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSgekmallekEILEKVNSPF-------IVSLAYAFET 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLQGGSILAHIQkqkHFNER--EASRVV---RDVAAALDFLHTKGIAHRDLKPENIL--CESPEKVSpvki 177
Cdd:cd05607    74 KTHLCLVMSLMNGGDLKYHIY---NVGERgiEMERVIfysAQITCGILHLHSLKIVYRDMKPENVLldDNGNCRLS---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 cdfDLGSGMKLNNSCTpittpeLTTPCGSAEYMAPEVVevfTDQAtfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcg 257
Cdd:cd05607   147 ---DLGLAVEVKEGKP------ITQRAGTNGYMAPEIL---KEES--YSYPVDWFAMGCSIYEMVAGRTPFRDHKEKV-- 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 258 wDRGEVCRvcqnKLFESiqEGKYEFPDkdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd05607   211 -SKEELKR----RTLED--EVKFEHQN-----FTEEAKDICRLFLAKKPENRLGSRTNDDDP 260
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
41-321 2.21e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 78.59  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII-EKQAGHSRSRVfrEVETLYQCQ-----GNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14225    49 EVIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRFHHQALV--EVKILDALRrkdrdNSHNVIHMKEYFYFRNHLCITFEL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LqgGSILAHIQKQKHFNEREASrVVRDVAAA----LDFLHTKGIAHRDLKPENILCESPEKVSpVKICDFdlGSgmklnn 190
Cdd:cd14225   127 L--GMNLYELIKKNNFQGFSLS-LIRRFAISllqcLRLLYRERIIHCDLKPENILLRQRGQSS-IKVIDF--GS------ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCtpITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD---C-----GWDRGE 262
Cdd:cd14225   195 SC--YEHQRVYTYIQSRFYRSPEVI-----LGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEqlaCimevlGLPPPE 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 263 VCRVCQNK--LFESI--------QEGKYEFPD-KDWAHI--SSEAK--DLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14225   268 LIENAQRRrlFFDSKgnprcitnSKGKKRRPNsKDLASAlkTSDPLflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-321 3.14e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 76.93  E-value: 3.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEK----QAGH--SRSRVFREVETLYQC-QGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14100     7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKdrvsEWGElpNGTRVPMEIVLLKKVgSGFRGVIRLLDWFERPDSFVLVLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQG-GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSGMKLNNSCt 193
Cdd:cd14100    87 PEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDL--NTGELKLIDF--GSGALLKDTV- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 194 pittpeLTTPCGSAEYMAPEVVEVFtdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcrvcqnKLFE 273
Cdd:cd14100   162 ------YTDFDGTRVYSPPEWIRFH----RYHGRSAAVWSLGILLYDMVCGDIPF---------------------EHDE 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14100   211 EIIRGQVFFRQR----VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
41-247 4.03e-16

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 77.40  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd06640    10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDlEEAEDEIEDIQQEITVLSQCD-SPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILaHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFdlGSGMKLNNsctpiTTPE 199
Cdd:cd06640    89 AL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADF--GVAGQLTD-----TQIK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPP 247
Cdd:cd06640   158 RNTFVGTPFWMAPEVI-----QQSAYDSKADIWSLGITAIELAKGEPP 200
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
40-319 5.04e-16

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 78.76  E-value: 5.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQaGHSRSRVFR---EVETLYQCqgnkNILELIEFFED----DTR----- 107
Cdd:PTZ00283   37 SRVLGSGATGTVLCAKRVSDGEPFAVKVVDME-GMSEADKNRaqaEVCCLLNC----DFFSIVKCHEDfakkDPRnpenv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 --FYLVFEKLQGGSILAHIQKQ----KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESpekvSPVKICDF 180
Cdd:PTZ00283  112 lmIALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANIlLCSN----GLVKLGDF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 DLgSGMKLNNSCTPITtpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdr 260
Cdd:PTZ00283  188 GF-SKMYAATVSDDVG----RTFCGTPYYVAPEIW-----RRKPYSKKADMFSLGVLLYELLTLKRPFDG---------- 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 261 gevcrvcqnklfESIQE-------GKYE-FPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:PTZ00283  248 ------------ENMEEvmhktlaGRYDpLPPS----ISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
43-321 5.23e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 76.62  E-value: 5.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd06645    19 IGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCK-HSNIVAYFGSYLRRDKLWICMEFCGGGSLQD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKlnnsctpITTPELTT 202
Cdd:cd06645    98 IYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN---GHVKLADFGVSAQIT-------ATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgWDRGEVcrvcqNKLFeSIQEGKYEF 282
Cdd:cd06645   168 FIGTPYWMAPEVAAV--ERKGGYNQLCDIWAVGITAIELAELQPPM---------FDLHPM-----RALF-LMTKSNFQP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1358101401 283 PD-KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06645   231 PKlKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
41-321 6.62e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 76.46  E-value: 6.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSR-VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKqIMSELEILYKCD-SPYIIGFYGAFFVENRISICTEFMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRdvaaALDFLHTKGIAHRDLKPENILCESPEKVspvKICDFdlGSGMKLNNSCTpittpe 199
Cdd:cd06619    86 LDVYRKIPEHVLGRIAVAVVK----GLTYLWSLKILHRDVKPSNMLVNTRGQV---KLCDF--GVSTQLVNSIA------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 lTTPCGSAEYMAPEvvEVFTDQatfYDKRCDLWSLGVVLYIMLSG---YPPFvghcgadcgwdRGEVCRVCQNKLFESI- 275
Cdd:cd06619   151 -KTYVGTNAYMAPE--RISGEQ---YGIHSDVWSLGISFMELALGrfpYPQI-----------QKNQGSLMPLQLLQCIv 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 276 QEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd06619   214 DEDPPVLPVGQF---SEKFVHFITQCMRKQPKERPAPENLMDHPFI 256
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
35-182 6.75e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 76.34  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  35 MYKLTsELLGEGAYAKVQGAVSLQNGKEYAVKIiEKQAgHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd14016     1 RYKLV-KKIGSGSFGEVYLGIDLKTGEEVAIKI-EKKD-SKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LqgGSILAHIQKQ--KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDL 182
Cdd:cd14016    78 L--GPSLEDLFNKcgRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGL 145
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
41-248 6.85e-16

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 76.63  E-value: 6.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIE-KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd06642    10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDlEEAEDEIEDIQQEITVLSQCD-SPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILaHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFdlGSGMKLNNsctpiTTPE 199
Cdd:cd06642    89 AL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLL---SEQGDVKLADF--GVAGQLTD-----TQIK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 200 LTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd06642   158 RNTFVGTPFWMAPEVI-----KQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
116-255 6.96e-16

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 75.89  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSgMKLNNSctp 194
Cdd:cd14062    71 EGSSLYKHLHVLEtKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLT---VKIGDFGLAT-VKTRWS--- 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 195 iTTPELTTPCGSAEYMAPEVVEVFTDqaTFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD 255
Cdd:cd14062   144 -GSQQFEQPTGSILWMAPEVIRMQDE--NPYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
145-320 8.22e-16

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 77.77  E-value: 8.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 145 ALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSGMKL---NNSCTPIttpelttpCgSAEYMAPEVVEvftdQ 221
Cdd:PTZ00036  182 ALAYIHSKFICHRDLKPQNLLIDP--NTHTLKLCDF--GSAKNLlagQRSVSYI--------C-SRFYRAPELML----G 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 222 ATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRVCQ---NKLFESIQE-----GKYEFPD---KDWAHI 290
Cdd:PTZ00036  245 ATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVD------QLVRIIQvlgTPTEDQLKEmnpnyADIKFPDvkpKDLKKV 318
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1358101401 291 -----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:PTZ00036  319 fpkgtPDDAINFISQFLKYEPLKRLNPIEALADPF 353
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
41-321 9.67e-16

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 76.91  E-value: 9.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS-----RVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14212     5 DLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQamleiAILTLLNTKYDPEDKHHIVRLLDHFMHHGHLCIVFELL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 qgGSILAHIQKQKHFNEREASRV---VRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFdlGSgmklnnSC 192
Cdd:cd14212    85 --GVNLYELLKQNQFRGLSLQLIrkfLQQLLDALSVLKDARIIHCDLKPENILLVNLDS-PEIKLIDF--GS------AC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 193 TPITTpeLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRVCQ---- 268
Cdd:cd14212   154 FENYT--LYTYIQSRFYRSPEVL-----LGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYN------QLSRIIEmlgm 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 269 ------------NKLFESIQ----EGKYEF---------------PDKDW--------------------AHISSEAK-- 295
Cdd:cd14212   221 ppdwmlekgkntNKFFKKVAksggRSTYRLktpeefeaenncklePGKRYfkyktlediimnypmkkskkEQIDKEMEtr 300
                         330       340       350
                  ....*....|....*....|....*....|
gi 1358101401 296 ----DLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14212   301 lafiDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
41-320 9.76e-16

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 76.00  E-value: 9.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL--- 115
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIrlDTETEGVPSTAIREISLLKELN-HPNIVKLLDVIHTENKLYLVFEFLhqd 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 --------QGGSILAHIQKQKHFNereasrvvrdVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMK 187
Cdd:cd07860    85 lkkfmdasALTGIPLPLIKSYLFQ----------LLQGLAFCHSHRVLHRDLKPQNLLINTEGA---IKLADFGLARAFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LnnsctPITTpeLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgevcrvc 267
Cdd:cd07860   152 V-----PVRT--YTHEVVTLWYRAPEILL----GCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEID------------ 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 268 qnKLF----------ESIQEGKYEFPD----------KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07860   209 --QLFrifrtlgtpdEVVWPGVTSMPDykpsfpkwarQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
28-322 1.10e-15

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 76.74  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  28 LPGKFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd07854     3 LGSRYMDLRPL-----GCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLD-HDNIVKVYEVLGPSGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 --------------FYLVFEKLQggSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVs 173
Cdd:cd07854    77 dltedvgsltelnsVYIVQEYME--TDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 174 pVKICDFDLGSGMKLNNSCTPITTPELTTPCgsaeYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCG 253
Cdd:cd07854   154 -LKIGDFGLARIVDPHYSHKGYLSEGLVTKW----YRSPRLLL----SPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 254 ADC------------GWDRGEVCRVCQNKLFESIQEGKYEFPDKdWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd07854   225 LEQmqlilesvpvvrEEDRNELLNVIPSFVRNDGGEPRRPLRDL-LPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303

                  .
gi 1358101401 322 Q 322
Cdd:cd07854   304 S 304
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
30-320 1.16e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 76.20  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYKLTSelLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVfREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd07871     2 GKLETYVKLDK--LGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAI-REVSLLKNLK-HANIVTLHDIIHTERC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQ----------GGSILAHIQKQKHFnereasRVVRdvaaALDFLHTKGIAHRDLKPENILCEspEKvSPVKI 177
Cdd:cd07871    78 LTLVFEYLDsdlkqyldncGNLMSMHNVKIFMF------QLLR----GLSYCHKRKILHRDLKPQNLLIN--EK-GELKL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CDFDLGSGmklnnscTPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD-- 255
Cdd:cd07871   145 ADFGLARA-------KSVPTKTYSNEVVTLWYRPPDVLL----GSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEel 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 256 ------CGWDRGEVCR-VCQNKLFESiqegkYEFPD-------KDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07871   214 hlifrlLGTPTEETWPgVTSNEEFRS-----YLFPQyraqpliNHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
36-321 1.27e-15

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 76.11  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTsELLGEGAYAKVQGAVSLQNG-KEYAVKIIE-----KQAGHsrsrvfREVETLYQCQGN-----KNILELIEFFED 104
Cdd:cd14135     2 YRVY-GYLGKGVFSNVVRARDLARGnQEVAIKIIRnnelmHKAGL------KELEILKKLNDAdpddkKHCIRLLRHFEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLqggsilahiqkqkHFNEREA-----------SRVVRDVAA----ALDFLHTKGIAHRDLKPENILCEsp 169
Cdd:cd14135    75 KNHLCLVFESL-------------SMNLREVlkkygknvglnIKAVRSYAQqlflALKHLKKCNILHADIKPDNILVN-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 170 EKVSPVKICDFdlGSGMklnnsctPITTPELTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFV 249
Cdd:cd14135   140 EKKNTLKLCDF--GSAS-------DIGENEITPYLVSRFYRAPEIILGLP-----YDYPIDMWSVGCTLYELYTGKILFP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 250 GH-------CGADC-GWDRGEVCRVC--------QNKLFESIQEGK-----------YEFPDKDWAHISSEA-------- 294
Cdd:cd14135   206 GKtnnhmlkLMMDLkGKFPKKMLRKGqfkdqhfdENLNFIYREVDKvtkkevrrvmsDIKPTKDLKTLLIGKqrlpdedr 285
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1358101401 295 ------KDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14135   286 kkllqlKDLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
43-322 1.47e-15

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 76.62  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFR---EVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHvkaERDILAEAD-NEWVVRLYYSFQDKDNLYFVMDYIPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSG-------------- 185
Cdd:cd05625    88 MMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGfrwthdskyyqsgd 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 ------MKLNNS--------CTPITTP------------ELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLY 239
Cdd:cd05625   165 hlrqdsMDFSNEwgdpencrCGDRLKPlerraarqhqrcLAHSLVGTPNYIAPEVL-----LRTGYTQLCDWWSVGVILF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 240 IMLSGYPPFVGHCGADcgwdrgevcrvCQNKLFEsiQEGKYEFPDKdwAHISSEAKDLISKlLVRDAKQRL---SAAQVL 316
Cdd:cd05625   240 EMLVGQPPFLAQTPLE-----------TQMKVIN--WQTSLHIPPQ--AKLSPEASDLIIK-LCRGPEDRLgknGADEIK 303

                  ....*.
gi 1358101401 317 QHPWVQ 322
Cdd:cd05625   304 AHPFFK 309
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
45-320 1.51e-15

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 75.72  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  45 EGAYAKVQGAVSLQNGKEYAVKII---EKQAGHSRSRVfREVETLYQCQgNKNILELIE--FFEDDTRFYLVFE----KL 115
Cdd:cd07843    15 EGTYGVVYRARDKKTGEIVALKKLkmeKEKEGFPITSL-REINILLKLQ-HPNIVTVKEvvVGSNLDKIYMVMEyvehDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QggSILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVS---PVKICDFDL----GSGMKl 188
Cdd:cd07843    93 K--SLMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLL------LNnrgILKICDFGLareyGSPLK- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 189 nnsctpittpELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwdRGEVCRVcq 268
Cdd:cd07843   162 ----------PYTQLVVTLWYRAPELLL----GAKEYSTAIDMWSVGCIFAELLTKKPLFPG---------KSEIDQL-- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 269 NKLF-------ESIQEGKYEFP---DKDWAH--------------ISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07843   217 NKIFkllgtptEKIWPGFSELPgakKKTFTKypynqlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
31-320 1.58e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 75.55  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRF 108
Cdd:cd07839     1 KYEKLEKI-----GEGTYGTVFKAKNRETHEIVALKRVrlDDDDEGVPSSALREICLLKELK-HKNIVRLYDVLHSDKKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQ----------GGSILAHIQKQKHFNereasrvvrdVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKIC 178
Cdd:cd07839    75 TLVFEYCDqdlkkyfdscNGDIDPEIVKSFMFQ----------LLKGLAFCHSHNVLHRDLKPQNLLI---NKNGELKLA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFDLGSGMKLnnsctPITtpelttpCGSAE-----YMAPEVVEvftdQATFYDKRCDLWSLGVVLYIML-SGYPPFVGHC 252
Cdd:cd07839   142 DFGLARAFGI-----PVR-------CYSAEvvtlwYRPPDVLF----GAKLYSTSIDMWSAGCIFAELAnAGRPLFPGND 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 253 GADcgwdrgEVCRVCqnKLF----ESIQEGKYEFPD----------KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQ 314
Cdd:cd07839   206 VDD------QLKRIF--RLLgtptEESWPGVSKLPDykpypmypatTSLVNVvpklNSTGRDLLQNLLVCNPVQRISAEE 277

                  ....*.
gi 1358101401 315 VLQHPW 320
Cdd:cd07839   278 ALQHPY 283
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
43-238 1.80e-15

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 74.83  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIiEKQAGHSRSrVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGS--- 119
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKE-LKRFDEQRS-FLKEVKLM-RRLSHPNILRFIGVCVKDNKLNFITEYVNGGTlee 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPE 199
Cdd:cd14065    78 LLKSMDEQ--LPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKKPDRKKR 155
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1358101401 200 LTTpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVL 238
Cdd:cd14065   156 LTV-VGSPYWMAPEML-----RGESYDEKVDVFSFGIVL 188
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
43-319 2.31e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 74.77  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYakvqGAVSLQNGKEYAVKIIEKQAGHSRSR------VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd08221     8 LGRGAF----GEAVLYRKTEDNSLVVWKEVNLSRLSekerrdALNEIDILSLLN-HDNIITYYNHFLDGESLFIEMEYCN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLNNSCTp 194
Cdd:cd08221    83 GGNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFL---TKADLVKLGDFGISKVLDSESSMA- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSgyppfvghcgadcgwdrgeVCRVCQN----K 270
Cdd:cd08221   159 ------ESIVGTPYYMSPELV-----QGVKYNFKSDIWAVGCVLYELLT-------------------LKRTFDAtnplR 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 271 LFESIQEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd08221   209 LAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERP 254
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
132-251 2.59e-15

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 75.18  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 132 EREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSpVKICDFDLGSGMKLNNSCTPITtpelttpcGSAEYM 210
Cdd:cd13989   101 ESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRVI-YKLIDLGYAKELDQGSLCTSFV--------GTLQYL 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 211 APEVVEvfTDQatfYDKRCDLWSLGVVLYIMLSGYPPFVGH 251
Cdd:cd13989   172 APELFE--SKK---YTCTVDYWSFGTLAFECITGYRPFLPN 207
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
44-258 5.78e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 73.45  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  44 GEGAYAKVQGAVSLQNGKEYAVKIIEKqaghsrsrVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAH 123
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLK--------IEKEAEIL-SVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 124 IQkQKHFNEREASRVV---RDVAAALDFLHTKG---IAHRDLKPENILCESPekvSPVKICDFdlgSGMKLNNSCTPITT 197
Cdd:cd14060    73 LN-SNESEEMDMDQIMtwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVIAAD---GVLKICDF---GASRFHSHTTHMSL 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 198 pelttpCGSAEYMAPEVVEVFTDQATfydkrCDLWSLGVVLYIMLSGYPPFVGHCGADCGW 258
Cdd:cd14060   146 ------VGTFPWMAPEVIQSLPVSET-----CDTYSYGVVLWEMLTREVPFKGLEGLQVAW 195
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-321 7.40e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 73.07  E-value: 7.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-----AGHSRSRVFREVETLYQC-QGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14102     7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKErvtewGTLNGVMVPLEIVLLKKVgSGFRGVIKLLDWYERPDGFLIVMERP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 Q-GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSGMKLNNSCtp 194
Cdd:cd14102    87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDL--RTGELKLIDF--GSGALLKDTV-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ittpeLTTPCGSAEYMAPEVVEVFtdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcrvcqnKLFES 274
Cdd:cd14102   161 -----YTDFDGTRVYSPPEWIRYH----RYHGRSATVWSLGVLLYDMVCGDIPF---------------------EQDEE 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 275 IQEGKYEFPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14102   211 ILRGRLYFRRR----VSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
36-320 8.19e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 73.53  E-value: 8.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYA----VKIIEKQAGHSRSRVfREVETLYQCQG--NKNILELIEF-----FED 104
Cdd:cd07862     3 YECVAEI-GEGAYGKVFKARDLKNGGRFValkrVRVQTGEEGMPLSTI-REVAVLRHLETfeHPNVVRLFDVctvsrTDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEKLQGgSILAHIQKQKhfNEREASRVVRDVA----AALDFLHTKGIAHRDLKPENILCESPEKvspVKICDF 180
Cdd:cd07862    81 ETKLTLVFEHVDQ-DLTTYLDKVP--EPGVPTETIKDMMfqllRGLDFLHSHRVVHRDLKPQNILVTSSGQ---IKLADF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 181 DLGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdr 260
Cdd:cd07862   155 GLARIYSFQMALTSVVV--------TLWYRAPEVL-----LQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVD----- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 261 gevcrvCQNKLFESIQEGKYEfpdkDWAH-----------------------ISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd07862   217 ------QLGKILDVIGLPGEE----DWPRdvalprqafhsksaqpiekfvtdIDELGKDLLLKCLTFNPAKRISAYSALS 286

                  ...
gi 1358101401 318 HPW 320
Cdd:cd07862   287 HPY 289
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
41-320 9.71e-15

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 73.33  E-value: 9.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKI--IEKQAGHSRSRVFREVETLYQCQGNKNILELI--EFFEDDTR--FYLVFEK 114
Cdd:cd07837     7 EKIGEGTYGKVYKARDKNTGKLVALKKtrLEMEEEGVPSTALREVSLLQMLSQSIYIVRLLdvEHVEENGKplLYLVFEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQggsilahiQKQKHF---------NEREASRVVR---DVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFDL 182
Cdd:cd07837    87 LD--------TDLKKFidsygrgphNPLPAKTIQSfmyQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGL--LKIADLGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLnnsctPIT--TPELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCgadcgwdr 260
Cdd:cd07837   157 GRAFTI-----PIKsyTHEIVT----LWYRAPEVLL----GSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDS-------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 261 gEVCRVCqnKLF-------ESIQEGK------YEFPD---KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07837   216 -ELQQLL--HIFrllgtpnEEVWPGVsklrdwHEYPQwkpQDLSRAvpdlEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
32-243 1.02e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 73.18  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELLGEGAYakvqGAVSL--------QNGKEYAVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFF 102
Cdd:cd05038     1 FEERHLKFIKQLGEGHF----GSVELcrydplgdNTGEQVAVKSLQPSGEEQHMSDFkREIEILRTLD-HEYIVKYKGVC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 EDDTR--FYLVFEKLQGGSILAHIQKQKHFNEReaSRVVR---DVAAALDFLHTKGIAHRDLKPENILCESpEKVspVKI 177
Cdd:cd05038    76 ESPGRrsLRLIMEYLPSGSLRDYLQRHRDQIDL--KRLLLfasQICKGMEYLGSQRYIHRDLAARNILVES-EDL--VKI 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 178 CDFDLGSGMKLNNSCTPITTPElTTPcgsAEYMAPEVVEvftdQATFYDKRcDLWSLGVVLYIMLS 243
Cdd:cd05038   151 SDFGLAKVLPEDKEYYYVKEPG-ESP---IFWYAPECLR----ESRFSSAS-DVWSFGVTLYELFT 207
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
43-180 1.20e-14

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 69.78  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQG-NKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGlELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 122 AHIQKQKHFnEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDF 180
Cdd:cd13968    81 AYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL-SEDGN--VKLIDF 135
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
42-248 1.40e-14

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 72.92  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKV-QGAVslqNGKEYAVKIIEKQAGHS----RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14158    22 KLGEGGFGVVfKGYI---NDKNVAVKKLAAMVDIStedlTKQFEQEIQVMAKCQ-HENLVELLGYSCDGPQLCLVYTYMP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKH---FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSPvKICDFdlGSGMKLNNSCT 193
Cdd:cd14158    98 NGSLLDRLACLNDtppLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLD--ETFVP-KISDF--GLARASEKFSQ 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 194 PITTPELTtpcGSAEYMAPEVV--EVftdqatfyDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14158   173 TIMTERIV---GTTAYMAPEALrgEI--------TPKSDIFSFGVVLLEIITGLPPV 218
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-246 1.90e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 72.78  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  76 RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GI 154
Cdd:cd06650    47 RNQIIRELQVLHECN-SPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 155 AHRDLKPENILCESPEKvspVKICDFDLgSGMKLNNSCTPITtpelttpcGSAEYMAPEVVevftdQATFYDKRCDLWSL 234
Cdd:cd06650   126 MHRDVKPSNILVNSRGE---IKLCDFGV-SGQLIDSMANSFV--------GTRSYMSPERL-----QGTHYSVQSDIWSM 188
                         170
                  ....*....|...
gi 1358101401 235 GVVLYIMLSG-YP 246
Cdd:cd06650   189 GLSLVEMAVGrYP 201
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
43-322 1.97e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 72.78  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKII----EKQaGHSRSRVfREVETLYQCQgNKNILELIEFFEDD--TRFYLVFEKLQ 116
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVrmdnERD-GIPISSL-REITLLLNLR-HPNIVELKEVVVGKhlDSIFLVMEYCE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 G--GSILAHIQKQkhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL-----CespekvspVKICDFDLGSgmKLN 189
Cdd:cd07845    92 QdlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLltdkgC--------LKIADFGLAR--TYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTPItTPELTTpcgsAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRVCQn 269
Cdd:cd07845   160 LPAKPM-TPKVVT----LWYRAPELLL----GCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIE------QLDLIIQ- 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 270 kLF----ESIQEG--------KYEFPDKDWAH-------ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd07845   224 -LLgtpnESIWPGfsdlplvgKFTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
43-322 2.01e-14

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 72.10  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIE---KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG-G 118
Cdd:cd06607     9 IGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQDIIKEVKFLRQLR-HPNTIEYKGCYLREHTAWLVMEYCLGsA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKqKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNNSCTpittp 198
Cdd:cd06607    88 SDIVEVHK-KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEP---GTVKLADFGSASLVCPANSFV----- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elttpcGSAEYMAPEVVeVFTDQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcQNKLFESIQEG 278
Cdd:cd06607   159 ------GTPYWMAPEVI-LAMDEGQ-YDGKVDVWSLGITCIELAERKPPLFNMNA--------------MSALYHIAQND 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 279 KYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06607   217 SPTLSSGEW---SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
64-248 2.50e-14

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 71.97  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  64 AVKIIE-KQAGHSRSRVFR-EVETLYQCQgNKNILELIEFFeddTR--FYLVFEKLQGGSILAHIQ-KQKHFNEREASRV 138
Cdd:cd14150    26 AVKILKvTEPTPEQLQAFKnEMQVLRKTR-HVNILLFMGFM---TRpnFAIITQWCEGSSLYRHLHvTETRFDTMQLIDV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 139 VRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSpVKICDFDLGSgMKLNNSctpiTTPELTTPCGSAEYMAPEVVEVf 218
Cdd:cd14150   102 ARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EGLT-VKIGDFGLAT-VKTRWS----GSQQVEQPSGSILWMAPEVIRM- 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 1358101401 219 tDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14150   173 -QDTNPYSFQSDVYAYGVVLYELMSGTLPY 201
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
43-325 2.83e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 72.38  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIE---KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG-G 118
Cdd:cd06633    29 IGHGSFGAVYFATNSHTNEVVAIKKMSysgKQTNEKWQDIIKEVKFLQQLK-HPNTIEYKGCYLKDHTAWLVMEYCLGsA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKqKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSCTPITTP 198
Cdd:cd06633   108 SDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ---VKLADF--GSASIASPANSFVGTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 elttpcgsaEYMAPEVVeVFTDQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrvcQNKLFESIQEG 278
Cdd:cd06633   182 ---------YWMAPEVI-LAMDEGQ-YDGKVDIWSLGITCIELAERKPPLFNMNA--------------MSALYHIAQND 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 279 KYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQ 325
Cdd:cd06633   237 SPTLQSNEW---TDSFRGFVDYCLQKIPQERPSSAELLRHDFVRRER 280
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
36-242 3.47e-14

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 72.20  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFRE-------------VETLYQC------------Q 90
Cdd:cd13977     2 YSLIREV-GRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREfwalssiqrqhpnVIQLEECvlqrdglaqrmsH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  91 GNKN---ILELIE-------FFEDDTRFYL--VFEKLQGGSILAHIQKQKHfNEREASRVVRDVAAALDFLHTKGIAHRD 158
Cdd:cd13977    81 GSSKsdlYLLLVEtslkgerCFDPRSACYLwfVMEFCDGGDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVHRD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 159 LKPENILCESPEKVSPVKICDFDL-----GSGMKLNNSCTpITTPELTTPCGSAEYMAPEVVEvftdqaTFYDKRCDLWS 233
Cdd:cd13977   160 LKPDNILISHKRGEPILKVADFGLskvcsGSGLNPEEPAN-VNKHFLSSACGSDFYMAPEVWE------GHYTAKADIFA 232

                  ....*....
gi 1358101401 234 LGVVLYIML 242
Cdd:cd13977   233 LGIIIWAMV 241
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
41-242 4.60e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 71.44  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVK-IIEKQAGHSRSRVFREVETLYQcqgnkniLE---LIEFF-------------- 102
Cdd:cd14048    12 QCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELAREKVLREVRALAK-------LDhpgIVRYFnawlerppegwqek 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 103 EDDTRFYLVFEKLQGGSILAHIQKQKHFNEREAS---RVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICD 179
Cdd:cd14048    85 MDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFvclNIFKQIASAVEYLHSKGLIHRDLKPSNVFF-SLDDV--VKVGD 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 180 FDLGSGMKLNNSCTPITTP-----ELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIML 242
Cdd:cd14048   162 FGLVTAMDQGEPEQTVLTPmpayaKHTGQVGTRLYMSPEQI-----HGNQYSEKVDIFALGLILFELI 224
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
41-320 4.60e-14

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 71.26  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQagHSRSRVF---REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd07844     6 DKLGEGSYATVYKGRSKLTGQLVALKEIRLE--HEEGAPFtaiREASLLKDLK-HANIVTLHDIIHTKKTLTLVFEYLDT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 ---------GSILaHIQKQKHFnereASRVVRdvaaALDFLHTKGIAHRDLKPENILC-ESPEkvspVKICDFDLGSGMK 187
Cdd:cd07844    83 dlkqymddcGGGL-SMHNVRLF----LFQLLR----GLAYCHQRRVLHRDLKPQNLLIsERGE----LKLADFGLARAKS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LnnsctPITT--PELTTpcgsAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD---------C 256
Cdd:cd07844   150 V-----PSKTysNEVVT----LWYRPPDVLLGSTE----YSTSLDMWGVGCIFYEMATGRPLFPGSTDVEdqlhkifrvL 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 257 GWDRGEVCR-VCQNKLFESIQEGKY--EFPDKDWAHIS--SEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07844   217 GTPTEETWPgVSSNPEFKPYSFPFYppRPLINHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-322 4.71e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 71.70  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  76 RSRVFREVETLYQCqgnkNILELIEF---FEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK 152
Cdd:cd06615    43 RNQIIRELKVLHEC----NSPYIVGFygaFYSDGEISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 153 -GIAHRDLKPENILCESPekvSPVKICDFDLgSGMkLNNSCTpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDL 231
Cdd:cd06615   119 hKIMHRDVKPSNILVNSR---GEIKLCDFGV-SGQ-LIDSMA-------NSFVGTRSYMSPERL-----QGTHYTVQSDI 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 232 WSLGVVLYIMLSG-YP---PfvghcgadcgwDRGEV-----CRVCQNKLFESIQEGKYEFPDK----------DW----- 287
Cdd:cd06615   182 WSLGLSLVEMAIGrYPippP-----------DAKELeamfgRPVSEGEAKESHRPVSGHPPDSprpmaifellDYivnep 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 288 ------AHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd06615   251 ppklpsGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
41-320 6.19e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 71.00  E-value: 6.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGg 118
Cdd:PLN00009    8 EKIGEGTYGVVYKARDRVTNETIALKKIrlEQEDEGVPSTAIREISLLKEMQ-HGNIVRLQDVVHSEKRLYLVFEYLDL- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHF--NEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSPVKICDFDLGSGMKLnnsctPIT 196
Cdd:PLN00009   86 DLKKHMDSSPDFakNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLID--RRTNALKLADFGLARAFGI-----PVR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 TpeLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwdrgEVCRVCQ--NKLFES 274
Cdd:PLN00009  159 T--FTHEVVTLWYRAPEILL----GSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEID------ELFKIFRilGTPNEE 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 275 IQEGKYEFPD----------KDWAHI----SSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:PLN00009  227 TWPGVTSLPDyksafpkwppKDLATVvptlEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
55-249 7.16e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 70.76  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  55 VSLQNGKEYAVKI-IEKQAGHSRSRVFREV-ETLYQCQGNKNILELIEFFED-DTRFYL-VFEK---LQGGSILAHIQkq 127
Cdd:cd14038    31 LSPKNRERWCLEIqIMKRLNHPNVVAARDVpEGLQKLAPNDLPLLAMEYCQGgDLRKYLnQFENccgLREGAILTLLS-- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 128 khfnereasrvvrDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKIcdFDLGSGMKLNNS--CTPITtpelttpcG 205
Cdd:cd14038   109 -------------DISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKI--IDLGYAKELDQGslCTSFV--------G 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1358101401 206 SAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFV 249
Cdd:cd14038   166 TLQYLAPELLE-----QQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
43-317 8.36e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 70.61  E-value: 8.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVK--IIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFeddtrfylvFEKLQggsI 120
Cdd:cd14049    14 LGKGGYGKVYKVRNKLDGQYYAIKkiLIKKVTKRDCMKVLREVKVLAGLQ-HPNIVGYHTAW---------MEHVQ---L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQ--------------KHFNERE-------------ASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvs 173
Cdd:cd14049    81 MLYIQMQlcelslwdwivernKRPCEEEfksapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 174 PVKICDFDLGSGMKLNNSC-----TPITTPELTTPCGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLyimLSGYPPF 248
Cdd:cd14049   159 HVRIGDFGLACPDILQDGNdsttmSRLNGLTHTSGVGTCLYAAPEQLE-----GSHYDFKSDMYSIGVIL---LELFQPF 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 249 vghcGADcgWDRGEVcrvcqnklFESIQEGKyeFPdKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd14049   231 ----GTE--MERAEV--------LTQLRNGQ--IP-KSLCKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
133-319 9.32e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 71.06  E-value: 9.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 133 REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvkiCDFDLGSGMklnnscTPITTPELTTPCGSAEYMAP 212
Cdd:PHA03209  157 DQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQV-----CIGDLGAAQ------FPVVAPAFLGLAGTVETNAP 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 213 EVVevftdQATFYDKRCDLWSLGVVLYIMLSgYPPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPD-------K 285
Cdd:PHA03209  226 EVL-----ARDKYNSKADIWSAGIVLFEMLA-YPSTIFEDPPSTPEEYVKSCHSHLLKIISTLKVHPEEFPRdpgsrlvR 299
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 286 DWAHISSEAKD-------------------LISKLLVRDAKQRLSAAQVLQHP 319
Cdd:PHA03209  300 GFIEYASLERQpytrypcfqrvnlpidgefLVHKMLTFDAAMRPSAEEILNYP 352
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
43-320 1.41e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 70.26  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQ-NGKEYAVKIIeKQAGHSRSRVFREVETLYQ-----CQGNKNILELIEFFEDDTRFYLVFEkLQ 116
Cdd:cd14213    20 LGEGAFGKVVECIDHKmGGMHVAVKIV-KNVDRYREAARSEIQVLEHlnttdPNSTFRCVQMLEWFDHHGHVCIVFE-LL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC----------------ESPEKVSPVKIC 178
Cdd:cd14213    98 GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrdERTLKNPDIKVV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFdlGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGW 258
Cdd:cd14213   178 DF--GSATYDDEHHSTLVS--------TRHYRAPEVI-----LALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 259 DRGEVCRVCQNKLFESIQEGKYEFPDK-DWAHISSEAK------------------------DLISKLLVRDAKQRLSAA 313
Cdd:cd14213   243 MMERILGPLPKHMIQKTRKRKYFHHDQlDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLD 322

                  ....*..
gi 1358101401 314 QVLQHPW 320
Cdd:cd14213   323 EALKHPF 329
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
43-322 1.64e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.48  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKqAGHSR---SRVFREVETLYQCQgNKNILELI--------EFFEDdtrFYLV 111
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIAN-AFDNRidaKRTLREIKLLRHLD-HENVIAIKdimppphrEAFND---VYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEkLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENIL----CEspekvspVKICDFDLGsgmK 187
Cdd:cd07858    88 YE-LMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLlnanCD-------LKICDFGLA---R 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 188 LNNSCTPITTPELTTpcgsAEYMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVghcGADCgwdrgevcrVC 267
Cdd:cd07858   157 TTSEKGDFMTEYVVT----RWYRAPELLLNCSE----YTTAIDVWSVGCIFAELLGRKPLFP---GKDY---------VH 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 268 QNKLFESI----QEGKYEFPDKD--------------------WAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd07858   217 QLKLITELlgspSEEDLGFIRNEkarryirslpytprqsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLA 295
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
43-309 2.17e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 69.67  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVK---IIEKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd08229    32 IGRGQFSEVYRATCLLDGVPVALKkvqIFDLMDAKARADCIKEIDLLKQLN-HPNVIKYYASFIEDNELNIVLELADAGD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 I---LAHIQKQKHF-NEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGsgmKLNNSCTPI 195
Cdd:cd08229   111 LsrmIKHFKKQKRLiPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLG---RFFSSKTTA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPELTTPcgsaEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGhcgadcgwDRGEVCRVCQNklfesI 275
Cdd:cd08229   185 AHSLVGTP----YYMSPERI-----HENGYNFKSDIWSLGCLLYEMAALQSPFYG--------DKMNLYSLCKK-----I 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1358101401 276 QEGKYefPDKDWAHISSEAKDLISKLLVRDAKQR 309
Cdd:cd08229   243 EQCDY--PPLPSDHYSEELRQLVNMCINPDPEKR 274
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
42-250 2.22e-13

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 68.96  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAvsLQNGKEYAVKII----EKQAGHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14061     1 VIGVGGFGKVYRG--IWRGEEVAVKAArqdpDEDISVTLENVRQEAR-LFWMLRHPNIIALRGVCLQPPNLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRdVAAALDFLHTKG---IAHRDLKPENILCESP-------EKVspVKICDFDLGSGMK 187
Cdd:cd14061    78 GALNRVLAGRKIPPHVLVDWAIQ-IARGMNYLHNEApvpIIHRDLKSSNILILEAienedleNKT--LKITDFGLAREWH 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 188 lnnsctpiTTPELTTpCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14061   155 --------KTTRMSA-AGTYAWMAPEVIKSST-----FSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
30-333 3.54e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 69.25  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYKLtsELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVfREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd07872     3 GKMETYIKL--EKLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAI-REVSLLKDLK-HANIVTLHDIVHTDKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQG---------GSILAhIQKQKHFnereasrvVRDVAAALDFLHTKGIAHRDLKPENILCEspEKvSPVKIC 178
Cdd:cd07872    79 LTLVFEYLDKdlkqymddcGNIMS-MHNVKIF--------LYQILRGLAYCHRRKVLHRDLKPQNLLIN--ER-GELKLA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFDLGSGmklnnscTPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD--- 255
Cdd:cd07872   147 DFGLARA-------KSVPTKTYSNEVVTLWYRPPDVLL----GSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDelh 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 256 -----CGWDRGEVCR-VCQNKLFESIQEGKYEfPDKDWAH---ISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ--GE 324
Cdd:cd07872   216 lifrlLGTPTEETWPgISSNDEFKNYNFPKYK-PQPLINHaprLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRslGT 294

                  ....*....
gi 1358101401 325 QQHNGPDAL 333
Cdd:cd07872   295 RIHSLPESI 303
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
30-318 4.34e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 68.11  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYK-LTSELLGEGAYAKVQGAVSLQNGkeyavkiiekqaghsRSRVFREVETLyQCQGNKNILELIEFFEDDTR- 107
Cdd:cd14033    12 GSFKTVYRgLDTETTVEVAWCELQTRKLSKGE---------------RQRFSEEVEML-KGLQHPNIVRFYDSWKSTVRg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 ---FYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPekVSPVKICDFDL 182
Cdd:cd14033    76 hkcIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGP--TGSVKIGDLGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLNNSCTPITTPElttpcgsaeYMAPEVVEvftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrge 262
Cdd:cd14033   154 ATLKRASFAKSVIGTPE---------FMAPEMYE------EKYDEAVDVYAFGMCILEMATSEYPY-------------- 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 263 vcRVCQN--KLFESIQEGKYefPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:cd14033   205 --SECQNaaQIYRKVTSGIK--PDSFYKVKVPELKEIIEGCIRTDKDERFTIQDLLEH 258
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
42-319 4.57e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 68.48  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVSLQNGKEYAVKIIE--KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGgS 119
Cdd:cd07848     8 VVGEGAYGVVLKCRHKETKEIVAIKKFKdsEENEEVKETTLRELKMLRTLK-QENIVELKEAFRRRGKLYLVFEYVEK-N 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKHFNEREASR-VVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTpittp 198
Cdd:cd07848    86 MLELLEEMPNGVPPEKVRsYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV---LKLCDFGFARNLSEGSNAN----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 199 eLTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVC---QNKLFESI 275
Cdd:cd07848   158 -YTEYVATRWYRSPELL-----LGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLpaeQMKLFYSN 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 276 QE-GKYEFP--------DKDWAHI-SSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd07848   232 PRfHGLRFPavnhpqslERRYLGIlSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
43-255 7.71e-13

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 67.37  E-value: 7.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-QGAVSLQNGKEY--AVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTrFYLVFEKLQGG 118
Cdd:cd05060     3 LGHGNFGSVrKGVYLMKSGKEVevAVKTLKQEHEKAGKKEFlREASVMAQLD-HPCIVRLIGVCKGEP-LMLVMELAPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTPITT- 197
Cdd:cd05060    81 PLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGMSRALGAGSDYYRATTa 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 198 ---PelttpcgsAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS-GYPPFVGHCGAD 255
Cdd:cd05060   158 grwP--------LKWYAPECINYGK-----FSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPE 206
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
42-317 8.19e-13

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 67.28  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVslQNGKEYAVKIIEKqagHSRSRVFREvETLYQCQGNKNilELIEFFEDDTR-FYLVFEKLQGGSI 120
Cdd:cd14068     1 LLGDGGFGSVYRAV--YRGEDVAVKIFNK---HTSFRLLRQ-ELVVLSHLHHP--SLVALLAAGTApRMLVMELAPKGSL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCES--PEKVSPVKICDFDLGsgmklnNSCTPITt 197
Cdd:cd14068    73 DALLQQDNaSLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlyPNCAIIAKIADYGIA------QYCCRMG- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 198 peLTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVcrvcQNKLFESIQE 277
Cdd:cd14068   146 --IKTSEGTPGFRAPEVAR----GNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAI----QGKLPDPVKE 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1358101401 278 -GKYEFPdkdwahissEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd14068   216 yGCAPWP---------GVEALIKDCLKENPQCRPTSAQVFD 247
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
28-316 8.88e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 69.38  E-value: 8.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   28 LPGKFEDMYKLTSEL-----LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR--SRVFREVETLYQCQgNKNILELIE 100
Cdd:PTZ00266     1 MPGKYDDGESRLNEYevikkIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKERekSQLVIEVNVMRELK-HKNIVRYID 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  101 FF--EDDTRFYLVFEKLQGGSILAHIQK-QKHFNEREASRVV---RDVAAALDFLHT-------KGIAHRDLKPENILCE 167
Cdd:PTZ00266    80 RFlnKANQKLYILMEFCDAGDLSRNIQKcYKMFGKIEEHAIVditRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  168 SP----EKVS---------PV-KICDFDLGSGM---KLNNSCTpittpelttpcGSAEYMAPEVVevfTDQATFYDKRCD 230
Cdd:PTZ00266   160 TGirhiGKITaqannlngrPIaKIGDFGLSKNIgieSMAHSCV-----------GTPYYWSPELL---LHETKSYDDKSD 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  231 LWSLGVVLYIMLSGYPPFvgHCGADCgwdrgevcrvcqNKLFESIQEGkyefPDKDWAHISSEAKDLISKLLVRDAKQRL 310
Cdd:PTZ00266   226 MWALGCIIYELCSGKTPF--HKANNF------------SQLISELKRG----PDLPIKGKSKELNILIKNLLNLSAKERP 287

                   ....*.
gi 1358101401  311 SAAQVL 316
Cdd:PTZ00266   288 SALQCL 293
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
43-320 9.50e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 68.11  E-value: 9.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGK-EYAVKIIeKQAGHSRSRVFREVETLY----QCQGNKNILELI-EFFEDDTRFYLVFEKLq 116
Cdd:cd14214    21 LGEGTFGKVVECLDHARGKsQVALKII-RNVGKYREAARLEINVLKkikeKDKENKFLCVLMsDWFNFHGHMCIAFELL- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 gGSILAHIQKQKHFNEREASRVvRDVA----AALDFLHTKGIAHRDLKPENIL---------------CESPE-KVSPVK 176
Cdd:cd14214    99 -GKNTFEFLKENNFQPYPLPHI-RHMAyqlcHALKFLHENQLTHTDLKPENILfvnsefdtlynesksCEEKSvKNTSIR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 177 ICDFdlGSGMklnnsctpITTPELTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD- 255
Cdd:cd14214   177 VADF--GSAT--------FDHEHHTTIVATRHYRPPEVILELG-----WAQPCDVWSLGCILFEYYRGFTLFQTHENREh 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 256 --------CGWDRGEVCRVCQNKLF--------ESIQEGKYE----FPDKDW-AHISSEAK---DLISKLLVRDAKQRLS 311
Cdd:cd14214   242 lvmmekilGPIPSHMIHRTRKQKYFykgslvwdENSSDGRYVsencKPLMSYmLGDSLEHTqlfDLLRRMLEFDPALRIT 321

                  ....*....
gi 1358101401 312 AAQVLQHPW 320
Cdd:cd14214   322 LKEALLHPF 330
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
41-243 1.08e-12

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 67.46  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAvSLQNgKEYAVKIIEKQaghSRSRVFREVEtLYQCQGNK--NILELIEFFEDDT----RFYLVFEK 114
Cdd:cd13998     1 EVIGKGRFGEVWKA-SLKN-EPVAVKIFSSR---DKQSWFREKE-IYRTPMLKheNILQFIAADERDTalrtELWLVTAF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKqkHFNEREAS-RVVRDVAAALDFLHTK---------GIAHRDLKPENILcespekvspVK------IC 178
Cdd:cd13998    75 HPNGSL*DYLSL--HTIDWVSLcRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNIL---------VKndgtccIA 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 179 DFDLGSGMKLNNSCTPI-TTPELttpcGSAEYMAPEVVEV---FTDQATFydKRCDLWSLGVVLYIMLS 243
Cdd:cd13998   144 DFGLAVRLSPSTGEEDNaNNGQV----GTKRYMAPEVLEGainLRDFESF--KRVDIYAMGLVLWEMAS 206
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
38-320 1.12e-12

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 67.29  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRS-RVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd07870     3 LNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPfTAIREASLLKGLK-HANIVLLHDIIHTKETLTFVFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSGMKLnnsctpit 196
Cdd:cd07870    82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISY---LGELKLADFGLARAKSI-------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 197 tpelttPCG--SAE-----YMAPEVVEVFTDqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgWDRGEVCRVCQN 269
Cdd:cd07870   151 ------PSQtySSEvvtlwYRPPDVLLGATD----YSSALDIWGAGCIFIEMLQGQPAFPGVSDV---FEQLEKIWTVLG 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 270 KLFESIQEGKYEFPDKD---------------WAHISS--EAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07870   218 VPTEDTWPGVSKLPNYKpewflpckpqqlrvvWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
41-255 1.29e-12

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 67.47  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFrEVETLYQCQGNK----NILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14211     5 EFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI-EVSILSRLSQENadefNFVRAYECFQHKNHTCLVFEMLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGsiLAHIQKQKHFNE---REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVS-PVKICDFdlgsgmklnNSC 192
Cdd:cd14211    84 QN--LYDFLKQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDF---------GSA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 193 TPITTPELTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGAD 255
Cdd:cd14211   153 SHVSKAVCSTYLQSRYYRAPEIILGLP-----FCEAIDMWSLGCVIAELFLGWPLYPGSSEYD 210
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
43-317 1.33e-12

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 67.15  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFF-----EDDTRF--YLVFEKL 115
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAAsigkeESDQGQaeYLLLTEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQK---QKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNN 190
Cdd:cd14036    88 CKGQLVDFVKKveaPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ---IKLCDF--GSATTEAH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 SCT-------------PITTpeLTTPCgsaeYMAPEVVEVFTDQATfyDKRCDLWSLGVVLYIMLsgyppFVGHCGADCG 257
Cdd:cd14036   163 YPDyswsaqkrslvedEITR--NTTPM----YRTPEMIDLYSNYPI--GEKQDIWALGCILYLLC-----FRKHPFEDGA 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 258 wdrgevcrvcqnKLfeSIQEGKYEFPDKDWAHisSEAKDLISKLLVRDAKQRLSAAQVLQ 317
Cdd:cd14036   230 ------------KL--RIINAKYTIPPNDTQY--TVFHDLIRSTLKVNPEERLSITEIVE 273
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
41-250 1.37e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 66.99  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVslQNGKEYAVKIIEKQAGHSRSRVF---REVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14145    12 EIIGIGGFGKVYRAI--WIGDEVAVKAARHDPDEDISQTIenvRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRdVAAALDFLHTKGIA---HRDLKPENILCEspEKVSP-------VKICDFDLGSGMK 187
Cdd:cd14145    90 GPLNRVLSGKRIPPDILVNWAVQ-IARGMNYLHCEAIVpviHRDLKSSNILIL--EKVENgdlsnkiLKITDFGLAREWH 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 188 LNNSctpittpelTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14145   167 RTTK---------MSAAGTYAWMAPEVI-----RSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-246 2.69e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 66.61  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  76 RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTK-GI 154
Cdd:cd06649    47 RNQIIRELQVLHECN-SPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 155 AHRDLKPENILCESPEKvspVKICDFDLgSGMKLNNSCTPITtpelttpcGSAEYMAPEVVevftdQATFYDKRCDLWSL 234
Cdd:cd06649   126 MHRDVKPSNILVNSRGE---IKLCDFGV-SGQLIDSMANSFV--------GTRSYMSPERL-----QGTHYSVQSDIWSM 188
                         170
                  ....*....|...
gi 1358101401 235 GVVLYIMLSG-YP 246
Cdd:cd06649   189 GLSLVELAIGrYP 201
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
41-243 3.68e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 65.86  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEY----AVKII---EKQAGHSRSRVFREVETLYqcqgnKNILELIEFFED----DTRFY 109
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKQNASGQyetvAVKIFpyeEYASWKNEKDIFTDASLKH-----ENILQFLTAEERgvglDRQYW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSiLAHIQKQKHFNEREASRVVRDVAAALDFLHTK---------GIAHRDLKPENILCESPEKVSpvkICDF 180
Cdd:cd14055    76 LITAYHENGS-LQDYLTRHILSWEDLCKMAGSLARGLAHLHSDrtpcgrpkiPIAHRDLKSSNILVKNDGTCV---LADF 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 181 dlGSGMKLNNSctpITTPELTTP--CGSAEYMAPEVVEV---FTDQATFydKRCDLWSLGVVLYIMLS 243
Cdd:cd14055   152 --GLALRLDPS---LSVDELANSgqVGTARYMAPEALESrvnLEDLESF--KQIDVYSMALVLWEMAS 212
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
43-320 3.82e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 65.51  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYA-VKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTR----FYLVFEKLQG 117
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESVLKgkkcIVLVTELMTS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPekVSPVKICDFDLGSGMKLNNSCTPI 195
Cdd:cd14031    98 GTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLATLMRTSFAKSVI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPelttpcgsaEYMAPEVVEvftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcRVCQN--KLFE 273
Cdd:cd14031   176 GTP---------EFMAPEMYE------EHYDESVDVYAFGMCMLEMATSEYPY----------------SECQNaaQIYR 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1358101401 274 SIQEGKYefPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14031   225 KVTSGIK--PASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
63-247 4.47e-12

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 65.50  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  63 YAVKIIEKQAGHSR-----SRVFREVETLYQCQgNKNILELIEFFE-DDTRFYLVFEKLqGGSILAHIQKQKH-----FN 131
Cdd:cd14001    31 WAVKKINSKCDKGQrslyqERLKEEAKILKSLN-HPNIVGFRAFTKsEDGSLCLAMEYG-GKSLNDLIEERYEaglgpFP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 132 EREASRVVRDVAAALDFLHT-KGIAHRDLKPENILCESPEKVspVKICDFdlGSGMKLNNSCTPITTPELTTpCGSAEYM 210
Cdd:cd14001   109 AATILKVALSIARALEYLHNeKKILHGDIKSGNVLIKGDFES--VKLCDF--GVSLPLTENLEVDSDPKAQY-VGTEPWK 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1358101401 211 APEVVE---VFTDQAtfydkrcDLWSLGVVLYIMLSGYPP 247
Cdd:cd14001   184 AKEALEeggVITDKA-------DIFAYGLVLWEMMTLSVP 216
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
137-251 5.92e-12

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 64.94  E-value: 5.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 137 RVVRDVAAALDFLHTKGIAHRDLKPENILCES--PEKVSPVKICDFdlgsGMKLNNSCTPITTPElttpcGSAEYMAPEV 214
Cdd:cd14000   116 RIALQVADGLRYLHSAMIIYRDLKSHNVLVWTlyPNSAIIIKIADY----GISRQCCRMGAKGSE-----GTPGFRAPEI 186
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1358101401 215 VEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGH 251
Cdd:cd14000   187 AR----GNVIYNEKVDVFSFGMLLYEILSGGAPMVGH 219
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
33-325 6.41e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 65.46  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSEL--LGEGAYAKVQGAVSLQNGKEYAVKIIE---KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd06635    21 EDPEKLFSDLreIGHGSFGAVYFARDVRTSEVVAIKKMSysgKQSNEKWQDIIKEVKFLQRIK-HPNSIEYKGCYLREHT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGG-SILAHIQKqKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGM 186
Cdd:cd06635   100 AWLVMEYCLGSaSDLLEVHK-KPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ---VKLADFGSASIA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 187 KLNNSCTpittpelttpcGSAEYMAPEVVeVFTDQATfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGadcgwdrgevcrv 266
Cdd:cd06635   176 SPANSFV-----------GTPYWMAPEVI-LAMDEGQ-YDGKVDVWSLGITCIELAERKPPLFNMNA------------- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 267 cQNKLFESIQEGKYEFPDKDWahiSSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGEQ 325
Cdd:cd06635   230 -MSALYHIAQNESPTLQSNEW---SDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRER 284
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
41-277 6.50e-12

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 64.99  E-value: 6.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYakvqGAVSLQN--GKEYAVKIIekqagHSRSRV--FREVEtLYQCQ--GNKNILELI--EFFEDD--TRFYL 110
Cdd:cd14056     1 KTIGKGRY----GEVWLGKyrGEKVAVKIF-----SSRDEDswFRETE-IYQTVmlRHENILGFIaaDIKSTGswTQLWL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLQGGSILAHIQKQKhFNEREASRVVRDVAAALDFLHTK--------GIAHRDLKPENILCEspekvSPVKICDFDL 182
Cdd:cd14056    71 ITEYHEHGSLYDYLQRNT-LDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVK-----RDGTCCIADL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 183 GSGMKLNNSCTPITTPElTTPCGSAEYMAPEVVEVfTDQATFYD--KRCDLWSLGVVLYIML----------SGYPPFVG 250
Cdd:cd14056   145 GLAVRYDSDTNTIDIPP-NPRVGTKRYMAPEVLDD-SINPKSFEsfKMADIYSFGLVLWEIArrceiggiaeEYQLPYFG 222
                         250       260
                  ....*....|....*....|....*..
gi 1358101401 251 HCGADCGWDRGEVCrVCQNKLFESIQE 277
Cdd:cd14056   223 MVPSDPSFEEMRKV-VCVEKLRPPIPN 248
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
33-248 7.33e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 65.04  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  33 EDMYKLTSEL--LGEGAYAKVQGAVSLQNGKEYAVKIIE---KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR 107
Cdd:cd06634    11 DDPEKLFSDLreIGHGSFGAVYFARDVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCYLREHT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQG-GSILAHIQKqKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGM 186
Cdd:cd06634    90 AWLVMEYCLGsASDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP---GLVKLGDFGSASIM 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 187 KLNNSCTpittpelttpcGSAEYMAPEVVeVFTDQATfYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd06634   166 APANSFV-----------GTPYWMAPEVI-LAMDEGQ-YDGKVDVWSLGITCIELAERKPPL 214
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
123-248 8.35e-12

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 64.68  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKhFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekvSPVKICDFDLGSGMKLNNscTPITTPELTT 202
Cdd:cd14063    88 HERKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN----GRVVITDFGLFSLSGLLQ--PGRREDTLVI 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 203 PCGSAEYMAPEVVEVFT-DQATF----YDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14063   161 PNGWLCYLAPEIIRALSpDLDFEeslpFTKASDVYAFGTVWYELLAGRWPF 211
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
43-248 9.80e-12

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 64.09  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSlqNGKEYAVKIIEKQAGHSRSRV---FREVETLyqCQGNK-NILELI-EFFEDDTRFYLVFEKLQG 117
Cdd:cd14064     1 IGSGSFGKVYKGRC--RNKIVAIKRYRANTYCSKSDVdmfCREVSIL--CRLNHpCVIQFVgACLDDPSQFAIVTQYVSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREAS-RVVRDVAAALDFLH--TKGIAHRDLKPENILCESPEKVSpvkICDFdlGSGMKLNNsctp 194
Cdd:cd14064    77 GSLFSLLHEQKRVIDLQSKlIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAV---VADF--GESRFLQS---- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 195 ITTPELTTPCGSAEYMAPevvEVFTdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14064   148 LDEDNMTKQPGNLRWMAP---EVFT-QCTRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
43-256 1.02e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 64.57  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQ----GAVSLQNGKEYAVKIIEKQAGHSRSR-VFREVETLYQCQgNKNILELIEFFEDD--TRFYLVFEKL 115
Cdd:cd05079    12 LGEGHFGKVElcryDPEGDNTGEQVAVKSLKPESGGNHIAdLKKEIEILRNLY-HENIVKYKGICTEDggNGIKLIMEFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTP 194
Cdd:cd05079    91 PSGSLKEYLPRNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKEYYT 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 195 ITTpELTTPcgsAEYMAPEVVEvftdQATFYdKRCDLWSLGVVLYIMLSgyppfvgHCGADC 256
Cdd:cd05079   168 VKD-DLDSP---VFWYAPECLI----QSKFY-IASDVWSFGVTLYELLT-------YCDSES 213
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
43-321 1.06e-11

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 64.77  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-QGAVSLQNGKEYAVKIIEKQAghsrsRVFREVEtLYQCQ-----GNKNILELIEFFEDDTR-------FY 109
Cdd:cd14013     3 LGEGGFGTVyKGSLLQKDPGGEKRRVVLKKA-----KEYGEVE-IWMNErvrraCPSSCAEFVGAFLDTTSkkftkpsLW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFeKLQGGSILAHIQKQKHF------------------NEREA---SRVVRDVAAALDFLHTKGIAHRDLKPENILCES 168
Cdd:cd14013    77 LVW-KYEGDATLADLMQGKEFpynlepiifgrvlipprgPKRENviiKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 169 PEKVspVKICDF----DLGSGMKLNNSCTpITTPELTTPcgsAEYMAPE---------VVEVFTDQATFYDK--RCDLWS 233
Cdd:cd14013   156 GDGQ--FKIIDLgaaaDLRIGINYIPKEF-LLDPRYAPP---EQYIMSTqtpsappapVAAALSPVLWQMNLpdRFDMYS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 234 LGVVLYIMLsgyppfVGHCGAD------------CGWDRGEVCRVCQNKLFESIQEGkYEFPDKDwahiSSEAKDLISKL 301
Cdd:cd14013   230 AGVILLQMA------FPNLRSDsnliafnrqlkqCDYDLNAWRMLVEPRASADLREG-FEILDLD----DGAGWDLVTKL 298
                         330       340
                  ....*....|....*....|
gi 1358101401 302 LVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14013   299 IRYKPRGRLSASAALAHPYF 318
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
41-250 1.30e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 64.66  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFrEVETLYQCQGNK----NILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14229     6 DFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI-EVGILARLSNENadefNFVRAYECFQHRNHTCLVFEMLE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGsiLAHIQKQKHFNE---REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14229    85 QN--LYDFLKQNKFSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVR-QPYRVKVIDFGSASHVSKTVC 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 194 pittpelTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14229   162 -------STYLQSRYYRAPEIILGLP-----FCEAIDMWSLGCVIAELFLGWPLYPG 206
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
41-250 1.81e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 64.34  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFrEVETL----YQCQGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14227    21 EFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI-EVSILarlsTESADDYNFVRAYECFQHKNHTCLVFEMLE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGsiLAHIQKQKHFNE---REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14227   100 QN--LYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSR-QPYRVKVIDFGSASHVSKAVC 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 194 pittpelTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14227   177 -------STYLQSRYYRAPEIILGLP-----FCEAIDMWSLGCVIAELFLGWPLYPG 221
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
43-238 1.87e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 63.44  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVM-RCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLgSGMKLNNSCTPITTPELT 201
Cdd:cd14221    80 IIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVV---VADFGL-ARLMVDEKTQPEGLRSLK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 202 TP--------CGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVL 238
Cdd:cd14221   156 KPdrkkrytvVGNPYWMAPEMI-----NGRSYDEKVDVFSFGIVL 195
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
43-246 1.99e-11

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 63.31  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAghSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG---S 119
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV--DQHKIVREISLLQKLS-HPNIVRYLGICVKDEKLHPILEYVSGGcleE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAhiQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMklnnSCTPITTPE 199
Cdd:cd14156    78 LLA--REELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREV----GEMPANDPE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1358101401 200 LT-TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYP 246
Cdd:cd14156   152 RKlSLVGSAFWMAPEML-----RGEPYDRKVDVFSFGIVLCEILARIP 194
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
38-248 2.10e-11

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 63.51  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQgavslqNGK---EYAVKIIE-KQAGHSRSRVFR-EVETLYQCQgNKNILELIEFFEDDTrFYLVF 112
Cdd:cd14149    15 MLSTRIGSGSFGTVY------KGKwhgDVAVKILKvVDPTPEQFQAFRnEVAVLRKTR-HVNILLFMGYMTKDN-LAIVT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSpVKICDFDLGSgMKLNNS 191
Cdd:cd14149    87 QWCEGSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLT-VKIGDFGLAT-VKSRWS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 192 ctpiTTPELTTPCGSAEYMAPEVVEVFTDQAtfYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14149   163 ----GSQQVEQPTGSILWMAPEVIRMQDNNP--FSFQSDVYSYGIVLYELMTGELPY 213
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
42-250 2.39e-11

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 63.13  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAVslQNGKEYAVKII----EKQAGHSRSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14146     1 IIGVGGFGKVYRAT--WKGQEVAVKAArqdpDEDIKATAESVRQEAK-LFSMLRHPNIIKLEGVCLEEPNLCLVMEFARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSI-LAHIQKQKHFNEREASRV--------VRDVAAALDFLHTKG---IAHRDLKPENILCEspEKVS-------PVKIC 178
Cdd:cd14146    78 GTLnRALAAANAAPGPRRARRIpphilvnwAVQIARGMLYLHEEAvvpILHRDLKSSNILLL--EKIEhddicnkTLKIT 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 179 DFDLGSGMKlnnsctpiTTPELTTpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14146   156 DFGLAREWH--------RTTKMSA-AGTYAWMAPEVI-----KSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
42-241 2.41e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 63.26  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAvsLQNGKEYAVKIIekqAGHSRSRVFREVEtLYQC--QGNKNILElieFFEDD-------TRFYLVF 112
Cdd:cd14144     2 SVGKGRYGEVWKG--KWRGEKVAVKIF---FTTEEASWFRETE-IYQTvlMRHENILG---FIAADikgtgswTQLYLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSILAHIQKQKhFNEREASRVVRDVAAALDFLHTK--------GIAHRDLKPENILcespekvspVK----ICDF 180
Cdd:cd14144    73 DYHENGSLYDFLRGNT-LDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNIL---------VKkngtCCIA 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 181 DLGSGMKLNNSCTPITTPeLTTPCGSAEYMAPEVVEVFTDQATFYD-KRCDLWSLGVVLYIM 241
Cdd:cd14144   143 DLGLAVKFISETNEVDLP-PNTRVGTKRYMAPEVLDESLNRNHFDAyKMADMYSFGLVLWEI 203
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
46-246 2.54e-11

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 62.95  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  46 GAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRvfrevETLYQcQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQ 125
Cdd:cd05576    10 GVIDKVLLVMDTRTQETFILKGLRKSSEYSRER-----KTIIP-RCVPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 126 KQkhFNEREASRVVRDVAA------------------------ALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFd 181
Cdd:cd05576    84 KF--LNDKEIHQLFADLDErlaaasrfyipeeciqrwaaemvvALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRW- 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 182 lgsgMKLNNSCtpittpelttpCGSA---EYMAPEVVEVFTDQATfydkrCDLWSLGVVLYIMLSGYP 246
Cdd:cd05576   161 ----SEVEDSC-----------DSDAienMYCAPEVGGISEETEA-----CDWWSLGALLFELLTGKA 208
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
43-320 2.80e-11

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 63.03  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVF------REVETLYQCQGNKNILELIEFFEDDTRF-----YLV 111
Cdd:cd14020     8 LGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQESgdygfaKERAALEQLQGHRNIVTLYGVFTNHYSAnvpsrCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKL--QGGSILAHIQKQKHfNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVspVKICDFDLgSGMKLN 189
Cdd:cd14020    88 LELLdvSVSELLLRSSNQGC-SMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDEC--FKLIDFGL-SFKEGN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTPITTPelttpcgsaEYMAPEV-VEVFTDQATF-YDKRC----DLWSLGVVLYIMLSGYppfvghcgadcgwdrgev 263
Cdd:cd14020   164 QDVKYIQTD---------GYRAPEAeLQNCLAQAGLqSETECtsavDLWSLGIVLLEMFSGM------------------ 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 264 crvcqnKLFESIQEgkYEFPDKDWA---HI-SSEA-----------KDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14020   217 ------KLKHTVRS--QEWKDNSSAiidHIfASNAvvnpaipayhlRDLIKSMLHNDPGKRATAEAALCSPF 280
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
30-320 3.16e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 63.17  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  30 GKFEDMYKLtsELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFY 109
Cdd:cd07869     2 GKADSYEKL--EKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSGmkln 189
Cdd:cd07869    80 LVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISD---TGELKLADFGLARA---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 nscTPITTPELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADcgwDRGEVCRVCQN 269
Cdd:cd07869   153 ---KSVPSHTYSNEVVTLWYRPPDVLL----GSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQ---DQLERIFLVLG 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 270 KLFESIQEGKYEFPD---------------KDWAHIS--SEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd07869   223 TPNEDTWPGVHSLPHfkperftlyspknlrQAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEY 290
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
41-239 4.28e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 62.84  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVslQNGKEYAVKIIEKQAGHSRsrvFREVEtLYQC--QGNKNILELIEFFEDD----TRFYLVFEK 114
Cdd:cd14143     1 ESIGKGRFGEVWRGR--WRGEDVAVKIFSSREERSW---FREAE-IYQTvmLRHENILGFIAADNKDngtwTQLWLVSDY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKhFNEREASRVVRDVAAALDFLH-----TKG---IAHRDLKPENILCESPEKVspvkiCDFDLGSGM 186
Cdd:cd14143    75 HEHGSLFDYLNRYT-VTVEGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDLKSKNILVKKNGTC-----CIADLGLAV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 187 KLNNSCTPITTPElTTPCGSAEYMAPEVVEVfTDQATFYD--KRCDLWSLGVVLY 239
Cdd:cd14143   149 RHDSATDTIDIAP-NHRVGTKRYMAPEVLDD-TINMKHFEsfKRADIYALGLVFW 201
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
41-250 4.52e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 63.18  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFrEVETLYQCQGNK----NILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14228    21 EFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQI-EVSILSRLSSENadeyNFVRSYECFQHKNHTCLVFEMLE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGsiLAHIQKQKHFNE---REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFDLGSGMKLNNSCT 193
Cdd:cd14228   100 QN--LYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVR-QPYRVKVIDFGSASHVSKAVC 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 194 pittpelTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14228   177 -------STYLQSRYYRAPEIILGLP-----FCEAIDMWSLGCVIAELFLGWPLYPG 221
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
58-255 5.12e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 63.71  E-value: 5.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401   58 QNGKEYAVKIIEKQAG---HSRSRVFREVETLYQCQgNKNILELIEFFE-DDTRFYLVFEKLQGGSILAHIQKQKHFNER 133
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPeeeHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  134 EASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLG---SGMKLNNSCTPITTPELTtpcGSAEYM 210
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGtllPGVRDADVATLTRTTEVL---GTPTYC 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1358101401  211 APEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLSGYPPFVGHCGAD 255
Cdd:TIGR03903  157 APEQLrgEPVTPNS-------DLYAWGLIFLECLTGQRVVQGASVAE 196
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
110-251 5.42e-11

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 62.24  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGSILAHIQKQKH---FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGM 186
Cdd:cd14039    73 LAMEYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDL 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 187 KLNNSCTPITtpelttpcGSAEYMAPEVVEvftdqATFYDKRCDLWSLGVVLYIMLSGYPPFVGH 251
Cdd:cd14039   153 DQGSLCTSFV--------GTLQYLAPELFE-----NKSYTVTVDYWSFGTMVFECIAGFRPFLHN 204
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
41-239 6.76e-11

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 62.07  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGavsLQNGKEYAVKIIEKQAGHSRsrvFREVETLYQCQ-GNKNILELI----EFFEDDTRFYLVFEK 114
Cdd:cd14142    11 ECIGKGRYGEVwRG---QWQGESVAVKIFSSRDEKSW---FRETEIYNTVLlRHENILGFIasdmTSRNSCTQLWLITHY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQKhFNEREASRVVRDVAAALDFLHTK--------GIAHRDLKPENILCEspekvSPVKICDFDLGSGM 186
Cdd:cd14142    85 HENGSLYDYLQRTT-LDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVK-----SNGQCCIADLGLAV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 187 kLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATFYD-KRCDLWSLGVVLY 239
Cdd:cd14142   159 -THSQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESyKRVDIYAFGLVLW 211
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
43-267 7.19e-11

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 61.76  E-value: 7.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIekqaghsRSRVFReVETLYQCQG--NKNILELIEFFEDDTRFYLVFEKLQGGSI 120
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKV-------RLEVFR-AEELMACAGltSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpeKVSPVKICDFdlGSGMKLNNSCTPITTPEL 200
Cdd:cd13991    86 GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSS--DGSDAFLCDF--GHAECLDPDGLGKSLFTG 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 201 TTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPfvghcgadcgWDRGEVCRVC 267
Cdd:cd13991   162 DYIPGTETHMAPEVV-----LGKPCDAKVDVWSSCCMMLHMLNGCHP----------WTQYYSGPLC 213
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
31-277 7.38e-11

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 61.94  E-value: 7.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDmykltseLLGEGAYAKVQGAVSLQNGKEY--AVKIIEKQAGHSRSRVFR-EVETLYQCQGNKNILELIEFFEDDTR 107
Cdd:cd05089     5 KFED-------VIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFAgELEVLCKLGHHPNIINLLGACENRGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQK----------------HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCesPEK 171
Cdd:cd05089    78 LYIAIEYAPYGNLLDFLRKSRvletdpafakehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLV--GEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 172 VSpVKICDFDLGSGMKLNNSCTPITTPelttpcgsAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLY--IMLSGYPpfv 249
Cdd:cd05089   156 LV-SKIADFGLSRGEEVYVKKTMGRLP--------VRWMAIESLNY-----SVYTTKSDVWSFGVLLWeiVSLGGTP--- 218
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1358101401 250 gHCGADC---------GWdRGEVCRVCQNKLFESIQE 277
Cdd:cd05089   219 -YCGMTCaelyeklpqGY-RMEKPRNCDDEVYELMRQ 253
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
41-316 9.93e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 61.60  E-value: 9.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEY--AVKIIEKQAGHSRSRVFR-EVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05047     1 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQK----------------HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSpvKICDFD 181
Cdd:cd05047    81 GNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV-GENYVA--KIADFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSGMKLNNSCTPITTPelttpcgsAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLY--IMLSGYPpfvgHCGADCGwd 259
Cdd:cd05047   158 LSRGQEVYVKKTMGRLP--------VRWMAIESLNY-----SVYTTNSDVWSYGVLLWeiVSLGGTP----YCGMTCA-- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 260 rgevcrvcqnKLFESIQEG-KYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVL 316
Cdd:cd05047   219 ----------ELYEKLPQGyRLEKP----LNCDDEVYDLMRQCWREKPYERPSFAQIL 262
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
43-238 1.01e-10

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 61.37  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVM-RSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQ-KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLNNSCTPITTPELT 201
Cdd:cd14154    80 VLKdMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVV---VADFGLARLIVEERLPSGNMSPSET 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 202 -------------TPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVL 238
Cdd:cd14154   157 lrhlkspdrkkryTVVGNPYWMAPEML-----NGRSYDEKVDIFSFGIVL 201
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
41-239 1.09e-10

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 61.61  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAvSLQNgKEYAVKIIekqAGHSRSRVFREVEtLYQCQG--NKNILELI-----EFFEDDTRFYLVFE 113
Cdd:cd14054     1 QLIGQGRYGTVWKG-SLDE-RPVAVKVF---PARHRQNFQNEKD-IYELPLmeHSNILRFIgaderPTADGRMEYLLVLE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSiLAHIQKQKHFNEREASRVVRDVAAALDFLHTK---------GIAHRDLKPENILcespekvspVK------IC 178
Cdd:cd14054    75 YAPKGS-LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVL---------VKadgscvIC 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 179 DFdlGSGMKLNNSCTPITTPELTTPCGSAE-----YMAPEVVE--VFTDQATFYDKRCDLWSLGVVLY 239
Cdd:cd14054   145 DF--GLAMVLRGSSLVRGRPGAAENASISEvgtlrYMAPEVLEgaVNLRDCESALKQVDVYALGLVLW 210
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
43-241 1.29e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 61.21  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQgaVSLQNGKEYAVKIIEKQaghSRSRVFREVEtLYQC--QGNKNILELI----EFFEDDTRFYLVFEKLQ 116
Cdd:cd14220     3 IGKGRYGEVW--MGKWRGEKVAVKVFFTT---EEASWFRETE-IYQTvlMRHENILGFIaadiKGTGSWTQLYLITDYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIqKQKHFNEREASRVVRDVAAALDFLHTK--------GIAHRDLKPENILCESPEKVspvkiCDFDLGSGMKL 188
Cdd:cd14220    77 NGSLYDFL-KCTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTC-----CIADLGLAVKF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 189 NNSCTPITTPeLTTPCGSAEYMAPEVVEVFTDQATFYDK-RCDLWSLGVVLYIM 241
Cdd:cd14220   151 NSDTNEVDVP-LNTRVGTKRYMAPEVLDESLNKNHFQAYiMADIYSFGLIIWEM 203
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
43-320 1.30e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 60.86  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIE--KQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTR----FYLVFEKLQ 116
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWVEVAWCELQdrKLTKVERQRFKEEAEMLKGLQ-HPNIVRFYDFWESCAKgkrcIVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPekVSPVKICDFDLGSGMKLNNSCTP 194
Cdd:cd14032    88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLATLKRASFAKSV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 195 ITTPelttpcgsaEYMAPEVVEvftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvGHCGADCGWDRGEVCRVcQNKLFES 274
Cdd:cd14032   166 IGTP---------EFMAPEMYE------EHYDESVDVYAFGMCMLEMATSEYPY-SECQNAAQIYRKVTCGI-KPASFEK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1358101401 275 IQEgkyefpdkdwahisSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:cd14032   229 VTD--------------PEIKEIIGECICKNKEERYEIKDLLSHAF 260
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
43-248 1.31e-10

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 60.97  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVsLQNGKEYAVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSI- 120
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHGFqAEIQTLGMIR-HRNIVRLRGYCSNPTTNLLVYEYMPNGSLg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 -LAH--IQKQKHFNEREASRVVRDVAAALDFLH---TKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKlnnsctP 194
Cdd:cd14664    79 eLLHsrPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFE---AHVADFGLAKLMD------D 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 195 ITTPELTTPCGSAEYMAPEVVEvfTDQAtfyDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14664   150 KDSHVMSSVAGSYGYIAPEYAY--TGKV---SEKSDVYSYGVVLLELITGKRPF 198
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
43-182 1.36e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 60.73  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIieKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEkLQGGSILA 122
Cdd:cd14017     8 IGGGGFGEIYKVRDVVDGEEVAMKV--ESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMT-LLGPNLAE 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 123 HI--QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPVKICDFDL 182
Cdd:cd14017    85 LRrsQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaIGRGPSDERTVYILDFGL 147
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
43-321 1.44e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 61.57  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVEtLYQCQGNKN--------ILELIEFFE----DDTRFYL 110
Cdd:cd14218    18 LGWGHFSTVWLCWDIQRKRFVALKVV-KSAVHYTETAVDEIK-LLKCVRDSDpsdpkretIVQLIDDFKisgvNGVHVCM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLqGGSILAHIQKQKHFNERE--ASRVVRDVAAALDFLHTK-GIAHRDLKPENILCE-------------------- 167
Cdd:cd14218    96 VLEVL-GHQLLKWIIKSNYQGLPLpcVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCvdegyvrrlaaeatiwqqag 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 168 -SPEKVSPVKIC--DFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEV-------VEVFTDQAtfYDKRCDLWSLGVV 237
Cdd:cd14218   175 aPPPSGSSVSFGasDFLVNPLEPQNADKIRVKIADLGNACWVHKHFTEDIqtrqyraLEVLIGAE--YGTPADIWSTACM 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 238 LYIMLSGYPPFVGHCGADCGWD-------------------------------RGEVCRVCQNK---LFESIQEgKYEFP 283
Cdd:cd14218   253 AFELATGDYLFEPHSGEDYTRDedhiahivellgdipphfalsgrysreyfnrRGELRHIKNLKhwgLYEVLVE-KYEWP 331
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1358101401 284 DKDWAHISseakDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14218   332 LEQAAQFT----DFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
31-320 1.50e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 61.61  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  31 KFEDMYKLTSELLGEGAYAKVQGAVSL--QNGKEYAVKIIEKqAGHSRSRVfREVETLYQCQgNKNILELIEFF--EDDT 106
Cdd:cd07868    13 RVEDLFEYEGCKVGRGTYGHVYKAKRKdgKDDKDYALKQIEG-TGISMSAC-REIALLRELK-HPNVISLQKVFlsHADR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 107 RFYLVFEKLQGGsiLAHI----------QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC--ESPEKvSP 174
Cdd:cd07868    90 KVWLLFDYAEHD--LWHIikfhraskanKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgEGPER-GR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 175 VKICdfDLGSGMKLNNSCTPITtpELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHC-- 252
Cdd:cd07868   167 VKIA--DMGFARLFNSPLKPLA--DLDPVVVTFWYRAPELLL----GARHYTKAIDIWAIGCIFAELLTSEPIF--HCrq 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 253 -----------------------GADCGWDrgEVCRVCQNK-LFESIQEGKY------EFPDKDWAHISSEAKDLISKLL 302
Cdd:cd07868   237 ediktsnpyhhdqldrifnvmgfPADKDWE--DIKKMPEHStLMKDFRRNTYtncsliKYMEKHKVKPDSKAFHLLQKLL 314
                         330
                  ....*....|....*...
gi 1358101401 303 VRDAKQRLSAAQVLQHPW 320
Cdd:cd07868   315 TMDPIKRITSEQAMQDPY 332
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
41-255 1.51e-10

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 60.82  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGK--EYAVKIIEK---QAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTrFYLVFEK 114
Cdd:cd05040     1 EKLGDGSFGVVrRGEWTTPSGKviQVAVKCLKSdvlSQPNAMDDFLKEVNAMHSLD-HPNLIRLYGVVLSSP-LMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCT 193
Cdd:cd05040    79 APLGSLLDRLRKDQgHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLMRALPQNEDHY 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 194 pITTPELTTP---CgsaeymAPEVVEV--FTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVGHCGAD 255
Cdd:cd05040   156 -VMQEHRKVPfawC------APESLKTrkFSHAS-------DVWMFGVTLWEMFTyGEEPWLGLNGSQ 209
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
139-248 1.63e-10

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 60.20  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 139 VRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFdlGSGMKLNNSCTPITTpelttpCGSAEYMAPEVVevf 218
Cdd:cd14059    87 SKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV---LKISDF--GTSKELSEKSTKMSF------AGTVAWMAPEVI--- 152
                          90       100       110
                  ....*....|....*....|....*....|
gi 1358101401 219 tdQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14059   153 --RNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
26-321 1.72e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 61.20  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  26 DSLPGKFEDMYKLtsellGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQGN-------KNILEL 98
Cdd:cd14216     6 DLFNGRYHVIRKL-----GWGHFSTVWLSWDIQGKRFVAMKVV-KSAEHYTETALDEIKLLKSVRNSdpndpnrEMVVQL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  99 IEFFE----DDTRFYLVFEKLqGGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILCESPEK 171
Cdd:cd14216    80 LDDFKisgvNGTHICMVFEVL-GHHLLKWIIKSNYqgLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVNEQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 172 -----------------VSP----------VKICDfdlgsgmkLNNSCTpiTTPELTTPCGSAEYMAPEVVevftdQATF 224
Cdd:cd14216   159 yirrlaaeatewqrnflVNPlepknaeklkVKIAD--------LGNACW--VHKHFTEDIQTRQYRSLEVL-----IGSG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 225 YDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWD-------------------------------RGEVCRVCQNK--- 270
Cdd:cd14216   224 YNTPADIWSTACMAFELATGDYLFEPHSGEDYSRDedhialiiellgkvprklivagkyskefftkKGDLKHITKLKpwg 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 271 LFESIQEgKYEFPDKDWAHISseakDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14216   304 LFEVLVE-KYEWSQEEAAGFT----DFLLPMLELIPEKRATAAECLRHPWL 349
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
129-317 1.95e-10

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 60.97  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 129 HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPV-KICDF-----DLGSGMKLnnsctPITTPELTT 202
Cdd:cd14018   134 TPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFgcclaDDSIGLQL-----PFSSWYVDR 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 203 PcGSAEYMAPEVVEVFTDQATFYD-KRCDLWSLGVVLYIMLSGYPPFVGHCGAdcgwdrgevcrvcqNKLFESIQEGkyE 281
Cdd:cd14018   209 G-GNACLMAPEVSTAVPGPGVVINySKADAWAVGAIAYEIFGLSNPFYGLGDT--------------MLESRSYQES--Q 271
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1358101401 282 FPDKDwAHISSEAKDLISKLLVRDAKQRLS---AAQVLQ 317
Cdd:cd14018   272 LPALP-SAVPPDVRQVVKDLLQRDPNKRVSarvAANVLH 309
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
41-250 2.01e-10

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 60.89  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV--QGAVSLQNGKEY----AVKIIEKQAG-HSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd05053    18 KPLGEGAFGQVvkAEAVGLDNKPNEvvtvAVKMLKDDATeKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVVVE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNERE---ASRVVRD-------------VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKI 177
Cdd:cd05053    98 YASKGNLREFLRARRPPGEEAspdDPRVPEEqltqkdlvsfayqVARGMEYLASKKCIHRDLAARNVLV-TEDNV--MKI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CDFDLGSGM-------KLNNSCTPIttpelttpcgsaEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPP 247
Cdd:cd05053   175 ADFGLARDIhhidyyrKTTNGRLPV------------KWMAPEALfdRVYTHQS-------DVWSFGVLLWeIFTLGGSP 235

                  ...
gi 1358101401 248 FVG 250
Cdd:cd05053   236 YPG 238
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
34-320 2.16e-10

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 60.85  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLTSELLGEGAYAKVQGAVSL--QNGKEYAVKIIEKqAGHSRSRVfREVETLYQCQgNKNILELIEFF--EDDTRFY 109
Cdd:cd07867     1 DLFEYEGCKVGRGTYGHVYKAKRKdgKDEKEYALKQIEG-TGISMSAC-REIALLRELK-HPNVIALQKVFlsHSDRKVW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 110 LVFEKLQGGsiLAHI----------QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC--ESPEKvSPVKI 177
Cdd:cd07867    78 LLFDYAEHD--LWHIikfhraskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgEGPER-GRVKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 178 CdfDLGSGMKLNNSCTPITtpELTTPCGSAEYMAPEVVEvftdQATFYDKRCDLWSLGVVLYIMLSGYPPFvgHCGADCG 257
Cdd:cd07867   155 A--DMGFARLFNSPLKPLA--DLDPVVVTFWYRAPELLL----GARHYTKAIDIWAIGCIFAELLTSEPIF--HCRQEDI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 258 WDRGEVCRVCQNKLFESIQegkyeFP-DKDWAHI----------------------------------SSEAKDLISKLL 302
Cdd:cd07867   225 KTSNPFHHDQLDRIFSVMG-----FPaDKDWEDIrkmpeyptlqkdfrrttyansslikymekhkvkpDSKVFLLLQKLL 299
                         330
                  ....*....|....*...
gi 1358101401 303 VRDAKQRLSAAQVLQHPW 320
Cdd:cd07867   300 TMDPTKRITSEQALQDPY 317
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
140-333 2.47e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.01  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 140 RDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvkiCDFDLGSGMKLNNSctpITTPELTTPCGSAEYMAPEVVEVFT 219
Cdd:PHA03207  192 RRLLEALAYLHGRGIIHRDVKTENIFLDEPENA-----VLGDFGAACKLDAH---PDTPQCYGWSGTLETNSPELLALDP 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 220 dqatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCG----------------WDRGEVCRVCQN-KLFESIQEGKYEF 282
Cdd:PHA03207  264 -----YCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSSSsqlrsiircmqvhpleFPQNGSTNLCKHfKQYAIVLRPPYTI 338
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 283 PD---KDWAHISSEAkdLISKLLVRDAKQRLSAAQVLQHPWVqgeqQHNGPDAL 333
Cdd:PHA03207  339 PPvirKYGMHMDVEY--LIAKMLTFDQEFRPSAQDILSLPLF----TKEPINLL 386
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
42-248 2.69e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 60.00  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  42 LLGEGAYAKVQGAvsLQNGKEYAVKII----EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd14148     1 IIGVGGFGKVYKG--LWRGEEVAVKAArqdpDEDIAVTAENVRQEARLFWMLQ-HPNIIALRGVCLNPPHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSiLAHIQKQKHFNEREASRVVRDVAAALDFLHTKG---IAHRDLKPENILCESP---EKVS--PVKICDFDLGSGMKln 189
Cdd:cd14148    78 GA-LNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienDDLSgkTLKITDFGLAREWH-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 190 nsctpiTTPELTTpCGSAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14148   155 ------KTTKMSA-AGTYAWMAPEVIRL-----SLFSKSSDVWSFGVLLWELLTGEVPY 201
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
41-250 2.77e-10

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 60.92  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKII--EKQAGHSRSRVFREVETLYQ--CQGNKNILELIEFFEDDTRFYLVFEKLq 116
Cdd:cd14224    71 KVIGKGSFGQVVKAYDHKTHQHVALKMVrnEKRFHRQAAEEIRILEHLKKqdKDNTMNVIHMLESFTFRNHICMTFELL- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 ggSILAH--IQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvSPVKICDFdlGSgmklnnSC 192
Cdd:cd14224   150 --SMNLYelIKKNKFqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGR-SGIKVIDF--GS------SC 218
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 193 tpITTPELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14224   219 --YEHQRIYTYIQSRFYRAPEVI-----LGARYGMPIDMWSFGCILAELLTGYPLFPG 269
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
94-248 2.78e-10

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 60.07  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  94 NILeLIEFFEDDTRFYLVFEKLQGGSILAHIQ-KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekv 172
Cdd:cd14151    65 NIL-LFMGYSTKPQLAIVTQWCEGSSLYHHLHiIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED--- 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 173 SPVKICDFDLGSgMKLNNSctpiTTPELTTPCGSAEYMAPEVVEVftDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14151   141 LTVKIGDFGLAT-VKSRWS----GSHQFEQLSGSILWMAPEVIRM--QDKNPYSFQSDVYAFGIVLYELMTGQLPY 209
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
117-319 3.19e-10

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 60.11  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQK----HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPVKI-CDFDLGSGMKLNN 190
Cdd:cd14051    84 GGSLADAISENEkageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIfISRTPNPVSSEEEeEDFEGEEDNPESN 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 191 S----------CTPITTPELTTpcGSAEYMAPEVV-EVFTDQAtfydkRCDLWSLGVVLYIMLSGYPpfVGHCGADcgWD 259
Cdd:cd14051   164 EvtykigdlghVTSISNPQVEE--GDCRFLANEILqENYSHLP-----KADIFALALTVYEAAGGGP--LPKNGDE--WH 232
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 260 RgevcrvcqnklfesIQEGKyeFPDKDwaHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14051   233 E--------------IRQGN--LPPLP--QCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
141-322 4.14e-10

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 59.64  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 141 DVAAALDFLH-TKGIAHRDLKPENILCESPekvSPVKICDFDL-----GSGMKLNNSCTPITT-PELTTPcgSAEYMAPE 213
Cdd:cd14011   122 QISEALSFLHnDVKLVHGNICPESVVINSN---GEWKLAGFDFcisseQATDQFPYFREYDPNlPPLAQP--NLNYLAPE 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 214 VVEVFTdqatfYDKRCDLWSLGVVLY-IMLSGYPPFvghcgaDCGWDRGEvcrvcqNKLFESiQEGKYEFPDKdwAHISS 292
Cdd:cd14011   197 YILSKT-----CDPASDMFSLGVLIYaIYNKGKPLF------DCVNNLLS------YKKNSN-QLRQLSLSLL--EKVPE 256
                         170       180       190
                  ....*....|....*....|....*....|
gi 1358101401 293 EAKDLISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:cd14011   257 ELRDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
41-250 6.50e-10

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 58.86  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAvSLQNGKEYAVKII-EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGS 119
Cdd:cd05085     2 ELLGKGNFGEVYKG-TLKDKTPVAVKTCkEDLPQELKIKFLSEARILKQYD-HPNIVKLIGVCTQRQPIYIVMELVPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIQKQKhfNEREASRVVR---DVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDL----------GSGM 186
Cdd:cd05085    80 FLSFLRKKK--DELKTKQLVKfslDAAAGMAYLESKNCIHRDLAARNCLVGEN---NALKISDFGMsrqeddgvysSSGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 187 KLnnscTPIttpelttpcgsaEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05085   155 KQ----IPI------------KWTAPEALNYGR-----YSSESDVWSFGILLWETFSlGVCPYPG 198
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
138-322 8.10e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 59.52  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 138 VVRDVAAALDFLHTKGIAHRDLKPENILCESPEkvspvKICDFDLGSGMKLNNSctpITTPELTTPCGSAEYMAPEVVev 217
Cdd:PHA03211  265 VARQLLSAIDYIHGEGIIHRDIKTENVLVNGPE-----DICLGDFGAACFARGS---WSTPFHYGIAGTVDTNAPEVL-- 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 218 ftdQATFYDKRCDLWSLGVVLYimlsgypPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKY---EFPDKDWAHISSEA 294
Cdd:PHA03211  335 ---AGDPYTPSVDIWSAGLVIF-------EAAVHTASLFSASRGDERRPYDAQILRIIRQAQVhvdEFPQHAGSRLVSQY 404
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 295 KD---------------------------LISKLLVRDAKQRLSAAQVLQHPWVQ 322
Cdd:PHA03211  405 RHraarnrrpaytrpawtryykldldveyLVCRALTFDGARRPSAAELLRLPLFQ 459
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
43-238 8.82e-10

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 58.26  E-value: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIieKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKM--NTLSSNRANMLREVQLMNRLS-HPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGM---KLNNSCTPITtpe 199
Cdd:cd14155    78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIpdySDGKEKLAVV--- 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1358101401 200 lttpcGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVL 238
Cdd:cd14155   155 -----GSPYWMAPEVL-----RGEPYNEKADVFSYGIIL 183
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
43-255 1.02e-09

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 58.44  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAV--SLQNGKEYAVKIIEKQAGHS--RSRVFREVETLYQCQgNKNILELIEFFEDDTrFYLVFEKLQGG 118
Cdd:cd05116     3 LGSGNFGTVKKGYyqMKKVVKTVAVKILKNEANDPalKDELLREANVMQQLD-NPYIVRMIGICEAES-WMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTPITtp 198
Cdd:cd05116    81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHY---AKISDFGLSKALRADENYYKAQ-- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 199 elTTPCGSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS-GYPPFVGHCGAD 255
Cdd:cd05116   156 --THGKWPVKWYAPECMNYYK-----FSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNE 206
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
32-320 1.08e-09

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 58.87  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELlGEGAYAKVQGAVS-LQNGKEYAVKIIE-----KQAGHSRSRVFREVETlyQCQGNKNI-LELIEFFED 104
Cdd:cd14215    10 LQERYEIVSTL-GEGTFGRVVQCIDhRRGGARVALKIIKnvekyKEAARLEINVLEKINE--KDPENKNLcVQMFDWFDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 105 DTRFYLVFEkLQGGSILAHIQKQKHFNE--REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPE------------ 170
Cdd:cd14215    87 HGHMCISFE-LLGLSTFDFLKENNYLPYpiHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynlekkrd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 171 ----KVSPVKICDFdlGSGMKLNNSCTPITTpelttpcgSAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLSGYP 246
Cdd:cd14215   166 ersvKSTAIRVVDF--GSATFDHEHHSTIVS--------TRHYRAPEVILELG-----WSQPCDVWSIGCIIFEYYVGFT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 247 PFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPDK-DW------------------AHISSEAK------DLISKL 301
Cdd:cd14215   231 LFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYHGRlDWdentsagryvrenckplrRYLTSEAEehhqlfDLIESM 310
                         330
                  ....*....|....*....
gi 1358101401 302 LVRDAKQRLSAAQVLQHPW 320
Cdd:cd14215   311 LEYEPSKRLTLAAALKHPF 329
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
43-238 1.31e-09

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 58.03  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSpvkICDFDLGSGMKLNNSCTPITTP---- 198
Cdd:cd14222    80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVV---VADFGLSRLIVEEKKKPPPDKPttkk 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 199 ---------ELTTPCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVL 238
Cdd:cd14222   157 rtlrkndrkKRYTVVGNPYWMAPEML-----NGKSYDEKVDIFSFGIVL 200
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
32-255 2.49e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 57.33  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  32 FEDMYKLTSELLGEGAYAKVQGAV--SLQN--GKEYAVKIIEKQAGHSRSRVFREVETLYQCQgNKNILEL--IEFFEDD 105
Cdd:cd14205     1 FEERHLKFLQQLGKGNFGSVEMCRydPLQDntGEVVAVKKLQHSTEEHLRDFEREIEILKSLQ-HDNIVKYkgVCYSAGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 106 TRFYLVFEKLQGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGS 184
Cdd:cd14205    80 RNLRLIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR---VKIGDFGLTK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 185 GMKLNNSCTPITTPelttpcGSAE--YMAPEVVevftdQATFYDKRCDLWSLGVVLYIML-----SGYPP--FVGHCGAD 255
Cdd:cd14205   157 VLPQDKEYYKVKEP------GESPifWYAPESL-----TESKFSVASDVWSFGVVLYELFtyiekSKSPPaeFMRMIGND 225
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
43-250 2.60e-09

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 57.50  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKE-----YAVKIIEKQAGHS-RSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05055    43 LGAGAFGKVVEATAYGLSKSdavmkVAVKMLKPTAHSSeREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKlnNSCTP 194
Cdd:cd05055   123 YGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKI--VKICDFGLARDIM--NDSNY 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 195 ITTPELTTPcgsAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05055   198 VVKGNARLP---VKWMAPESIfnCVYTFES-------DVWSYGILLWEIFSlGSNPYPG 246
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
43-250 3.32e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 57.33  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKE-------YAVKIIEKQAGHSR-SRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd05098    21 LGEGCFGQVVLAEAIGLDKDkpnrvtkVAVKMLKSDATEKDlSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK----------------HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKIC 178
Cdd:cd05098   101 ASKGNLREYLQARRppgmeycynpshnpeeQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED---NVMKIA 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 179 DFDLGSGMKLNNSCTPITTPELttpcgSAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05098   178 DFGLARDIHHIDYYKKTTNGRL-----PVKWMAPEALfdRIYTHQS-------DVWSFGVLLWeIFTLGGSPYPG 240
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
64-243 3.73e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 56.95  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  64 AVKII---EKQAGHSRSRVFREVETLYqcqgnKNILELI----EFFEDDTRFYLVFEKLQGGSiLAHIQKQKHFNEREAS 136
Cdd:cd14053    22 AVKIFplqEKQSWLTEREIYSLPGMKH-----ENILQFIgaekHGESLEAEYWLITEFHERGS-LCDYLKGNVISWNELC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 137 RVVRDVAAALDFLHT----------KGIAHRDLKPENILCEspekvSPVKICDFDLGSGMKLNNSctpITTPELTTPCGS 206
Cdd:cd14053    96 KIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLK-----SDLTACIADFGLALKFEPG---KSCGDTHGQVGT 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1358101401 207 AEYMAPEVVE---VFTDQAtFydKRCDLWSLGVVLYIMLS 243
Cdd:cd14053   168 RRYMAPEVLEgaiNFTRDA-F--LRIDMYAMGLVLWELLS 204
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
40-250 3.82e-09

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 56.66  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKV-QGAVSLQNGKE--YAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTrFYLVFEKLQ 116
Cdd:cd05056    11 GRCIGEGQFGDVyQGVYMSPENEKiaVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIVMELAP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKhfNEREASRVVR---DVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGM------K 187
Cdd:cd05056    90 LGELRSYLQVNK--YSLDLASLILyayQLSTALAYLESKRFVHRDIAARNVLVSSPDC---VKLGDFGLSRYMedesyyK 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 188 LNNSCTPIttpelttpcgsaEYMAPEVVEV--FTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05056   165 ASKGKLPI------------KWMAPESINFrrFTSAS-------DVWMFGVCMWeILMLGVKPFQG 211
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
113-251 4.69e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 56.51  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 113 EKLQGGSI--LAHIQKQKhfnereasrVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLG-SGMKLN 189
Cdd:cd14067   101 ENHKGSSFmpLGHMLTFK---------IAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVQEHINIKLSDYGiSRQSFH 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 190 NSCTPITtpelttpcGSAEYMAPEVvevftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGH 251
Cdd:cd14067   172 EGALGVE--------GTPGYQAPEI-----RPRIVYDEKVDMFSYGMVLYELLSGQRPSLGH 220
pknD PRK13184
serine/threonine-protein kinase PknD;
142-248 4.83e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.86  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMK--------LNNSCTPITTPELTTP---CGSAEYM 210
Cdd:PRK13184  122 ICATIEYVHSKGVLHRDLKPDNILL---GLFGEVVILDWGAAIFKKleeedlldIDVDERNICYSSMTIPgkiVGTPDYM 198
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1358101401 211 APEvvEVFTDQATfydKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:PRK13184  199 APE--RLLGVPAS---ESTDIYALGVILYQMLTLSFPY 231
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
92-248 5.23e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 56.35  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  92 NKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREAsRVVRDVAAALDFLHTKGIAHRDLKPENILCespEK 171
Cdd:cd14027    50 HSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKG-RIILEIIEGMAYLHGKGVIHKDLKPENILV---DN 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 172 VSPVKICDFDLGSG---MKLNNSCTPITTpELTTPC----GSAEYMAPEVVEVFTDQATfydKRCDLWSLGVVLYIMLSG 244
Cdd:cd14027   126 DFHIKIADLGLASFkmwSKLTKEEHNEQR-EVDGTAkknaGTLYYMAPEHLNDVNAKPT---EKSDVYSFAIVLWAIFAN 201

                  ....
gi 1358101401 245 YPPF 248
Cdd:cd14027   202 KEPY 205
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
94-248 8.92e-09

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 55.32  E-value: 8.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  94 NILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQ-KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENilCESPEKv 172
Cdd:cd05084    55 NIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEgPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARN--CLVTEK- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 173 SPVKICDFDLG-----------SGMKLnnscTPIttpelttpcgsaEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIM 241
Cdd:cd05084   132 NVLKISDFGMSreeedgvyaatGGMKQ----IPV------------KWTAPEALNYGR-----YSSESDVWSFGILLWET 190

                  ....*...
gi 1358101401 242 LS-GYPPF 248
Cdd:cd05084   191 FSlGAVPY 198
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
137-250 2.60e-08

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 54.04  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 137 RVVRDVAAALDFLHTKG--IAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSctpiTTPELTTPCGSAEYMAPev 214
Cdd:cd14025    96 RIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYH---VKISDFGLAKWNGLSHS----HDLSRDGLRGTIAYLPP-- 166
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 215 vEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14025   167 -ERFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAG 201
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
43-248 3.31e-08

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 53.90  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIieKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDtRFYLVFEKLQGGSI-- 120
Cdd:cd14129     8 IGGGGFGEIYDALDLLTRENVALKV--ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRND-RFNYVVMQLQGRNLad 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 121 LAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPVKICDFdlGSGMKLNNSCTPITTPE 199
Cdd:cd14129    85 LRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDF--GLARQFTNSCGDVRPPR 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1358101401 200 LTTPC-GSAEYMApevveVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14129   163 AVAGFrGTVRYAS-----INAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 207
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
41-250 3.58e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 53.88  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAvslQNGKEYAVKIIEKQAGHSRSRVFREVET---LYQCQGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14147     9 EVIGIGGFGKVyRGS---WRGELVAVKAARQDPDEDISVTAESVRQearLFAMLAHPNIIALKAVCLEEPNLCLVMEYAA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSI---LAHIQKQKHFNEREASRVVRdvaaALDFLHTKGIA---HRDLKPENILCESP------EKVSpVKICDFDLGS 184
Cdd:cd14147    86 GGPLsraLAGRRVPPHVLVNWAVQIAR----GMHYLHCEALVpviHRDLKSNNILLLQPienddmEHKT-LKITDFGLAR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 185 GMKlnnsctpiTTPELTTpCGSAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14147   161 EWH--------KTTQMSA-AGTYAWMAPEVI-----KASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
41-316 5.42e-08

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 53.46  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNG--KEYAVKIIEKQAGHSRSRVFR-EVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05088    13 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKEYASKDDHRDFAgELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVR----------------DVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFD 181
Cdd:cd05088    93 GNLLDFLRKSRVLETDPAFAIANstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 182 LGSGMKLNNSCTPITTPelttpcgsAEYMAPEVVEVftdqaTFYDKRCDLWSLGVVLY--IMLSGYPpfvgHCGADCGwd 259
Cdd:cd05088   170 LSRGQEVYVKKTMGRLP--------VRWMAIESLNY-----SVYTTNSDVWSYGVLLWeiVSLGGTP----YCGMTCA-- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 260 rgevcrvcqnKLFESIQEG-KYEFPdkdwAHISSEAKDLISKLLVRDAKQRLSAAQVL 316
Cdd:cd05088   231 ----------ELYEKLPQGyRLEKP----LNCDDEVYDLMRQCWREKPYERPSFAQIL 274
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
43-324 7.27e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 53.13  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYA-VKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTR----FYLVFEKLQG 117
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAwCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKG--IAHRDLKPENILCESPekVSPVKICDFDLGSGMKLNNSCTPI 195
Cdd:cd14030   113 GTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLATLKRASFAKSVI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPelttpcgsaEYMAPEVVEvftdqaTFYDKRCDLWSLGVVLYIMLSGYPPFvghcgadcgwdrgevcRVCQN--KLFE 273
Cdd:cd14030   191 GTP---------EFMAPEMYE------EKYDESVDVYAFGMCMLEMATSEYPY----------------SECQNaaQIYR 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 274 SIQEG-------KYEFPdkdwahissEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:cd14030   240 RVTSGvkpasfdKVAIP---------EVKEIIEGCIRQNKDERYAIKDLLNHAFFQEE 288
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
43-324 9.36e-08

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 53.26  E-value: 9.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAY------------AKVQGAVSLQNGKEY-AVKIiekqagHSRSRVFRevetlyQCQgnKNILELIEFF------E 103
Cdd:PLN03225  140 LGEGAFgvvykaslvnkqSKKEGKYVLKKATEYgAVEI------WMNERVRR------ACP--NSCADFVYGFlepvssK 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFeKLQGGSILAHIQKQKHF------------------NEREA---SRVVRDVAAALDFLHTKGIAHRDLKPE 162
Cdd:PLN03225  206 KEDEYWLVW-RYEGESTLADLMQSKEFpynvepyllgkvqdlpkgLERENkiiQTIMRQILFALDGLHSTGIVHRDVKPQ 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 163 NILCEspEKVSPVKIcdFDLGSGMKLNNSCTPITTPELTTPcgsaEYMAPEVVEVFTD------------------QATF 224
Cdd:PLN03225  285 NIIFS--EGSGSFKI--IDLGAAADLRVGINYIPKEFLLDP----RYAAPEQYIMSTQtpsapsapvatalspvlwQLNL 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 225 YDkRCDLWSLGVVLYIML-------SGYPPF---VGHCGADCGWDRGEVcrvcQNKLFESIQEGkYEFPDKD----Wahi 290
Cdd:PLN03225  357 PD-RFDIYSAGLIFLQMAfpnlrsdSNLIQFnrqLKRNDYDLVAWRKLV----EPRASPDLRRG-FEVLDLDggagW--- 427
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1358101401 291 sseakDLISKLLVRDAKQRLSAAQVLQHPWVQGE 324
Cdd:PLN03225  428 -----ELLKSMMRFKGRQRISAKAALAHPYFDRE 456
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
142-250 1.28e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 52.70  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKLNnsctpittPELTTPcGSA----EYMAPEvvEV 217
Cdd:cd14207   189 VARGMEFLSSRKCIHRDLAARNILL-SENNV--VKICDFGLARDIYKN--------PDYVRK-GDArlplKWMAPE--SI 254
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1358101401 218 FTdqaTFYDKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd14207   255 FD---KIYSTKSDVWSYGVLLWEIFSlGASPYPG 285
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
43-250 2.10e-07

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 51.89  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEY-------AVKIIEKQAGHSR-SRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd05099    20 LGEGCFGQVVRAEAYGIDKSRpdqtvtvAVKMLKDNATDKDlADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIVEY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK------HFNEREASR----------VVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKIC 178
Cdd:cd05099   100 AAKGNLREFLRARRppgpdyTFDITKVPEeqlsfkdlvsCAYQVARGMEYLESRRCIHRDLAARNVLV-TEDNV--MKIA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 179 DFDLGSGM-------KLNNSCTPIttpelttpcgsaEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPF 248
Cdd:cd05099   177 DFGLARGVhdidyykKTSNGRLPV------------KWMAPEALfdRVYTHQS-------DVWSFGILMWeIFTLGGSPY 237

                  ..
gi 1358101401 249 VG 250
Cdd:cd05099   238 PG 239
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
38-319 2.59e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 51.08  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  38 LTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQ-AGHSRSRV-FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14139     3 LELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPfAGSSNEQLaLHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQ----KHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENI-LCESPEKVSPV-----KICDFDLGSG 185
Cdd:cd14139    83 NGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIfICHKMQSSSGVgeevsNEEDEFLSAN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 186 M--KLNN--SCTPITTPELTTpcGSAEYMAPEVVEvftDQATFYDKrCDLWSLGvvLYIMLSGYPPFVGHCGADcgWDRg 261
Cdd:cd14139   163 VvyKIGDlgHVTSINKPQVEE--GDSRFLANEILQ---EDYRHLPK-ADIFALG--LTVALAAGAEPLPTNGAA--WHH- 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 262 evcrvcqnklfesIQEGkyEFPDKDwAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14139   232 -------------IRKG--NFPDVP-QELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
43-250 2.70e-07

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 51.23  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-QGAVSLQNGK----EYAVKIIEKQAGHSRSRVFrEVETLYQCQGN-KNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05036    14 LGQGAFGEVyEGTVSGMPGDpsplQVAVKTLPELCSEQDEMDF-LMEALIMSKFNhPNIVRCIGVCFQRLPRFILLELMA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREAS-------RVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFdlgsGMKLN 189
Cdd:cd05036    93 GGDLKSFLRENRPRPEQPSSltmldllQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKIGDF----GMARD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 190 nsctpITTPELTTPCGSA----EYMAPEVVE--VFTdqatfydKRCDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05036   169 -----IYRADYYRKGGKAmlpvKWMPPEAFLdgIFT-------SKTDVWSFGVLLWeIFSLGYMPYPG 224
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
34-248 2.79e-07

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 51.03  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  34 DMYKLT-SELLGEGAYAKV-QGAVSlqnGKEYAVKIIE----KQAGHSRSRVFREVEtlyqcqgNKNILELIEFFEDDTr 107
Cdd:cd05083     4 NLQKLTlGEIIGEGEFGAVlQGEYM---GQKVAVKNIKcdvtAQAFLEETAVMTKLQ-------HKNLVRLLGVILHNG- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQKHF--NEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSpvKICDFDLGSG 185
Cdd:cd05083    73 LYIVMELMSKGNLVNFLRSRGRAlvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILV-SEDGVA--KISDFGLAKV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 186 --MKLNNSCTPIttpelttpcgsaEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLS-GYPPF 248
Cdd:cd05083   150 gsMGVDNSRLPV------------KWTAPEAL-----KNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
37-250 2.90e-07

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 51.17  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  37 KLT-SELLGEGAYAKVQGAVSLQNGKE-------YAVKIIEKQAGHSR-SRVFREVETLYQCQGNKNILELIEFFEDDTR 107
Cdd:cd05101    25 KLTlGKPLGEGCFGQVVMAEAVGIDKDkpkeavtVAVKMLKDDATEKDlSDLVSEMEMMKMIGKHKNIINLLGACTQDGP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQKHFNEREASRVVR----------------DVAAALDFLHTKGIAHRDLKPENILCespEK 171
Cdd:cd05101   105 LYVIVEYASKGNLREYLRARRPPGMEYSYDINRvpeeqmtfkdlvsctyQLARGMEYLASQKCIHRDLAARNVLV---TE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 172 VSPVKICDFDLGSgmKLNNSCTPITTPELTTPcgsAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPF 248
Cdd:cd05101   182 NNVMKIADFGLAR--DINNIDYYKKTTNGRLP---VKWMAPEALfdRVYTHQS-------DVWSFGVLMWeIFTLGGSPY 249

                  ..
gi 1358101401 249 VG 250
Cdd:cd05101   250 PG 251
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
43-244 3.02e-07

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 51.04  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQgAVSLQNgKEYAVKIIEK----QAGHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14160     1 IGEGEIFEVY-RVRIGN-RSYAVKLFKQekkmQWKKHWKRFLSELEVL-LLFQHPNILELAAYFTETEKFCLVYPYMQNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SILAHIQKQ---KHFNEREASRVVRDVAAALDFLHTK---GIAHRDLKPENILCEspEKVSPvKICDFDLG--SGMKLNN 190
Cdd:cd14160    78 TLFDRLQCHgvtKPLSWHERINILIGIAKAIHYLHNSqpcTVICGNISSANILLD--DQMQP-KLTDFALAhfRPHLEDQ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 191 SCTPITTPELTTPCGsaeYMAPEVVEvftdQATFYDKrCDLWSLGVVLYIMLSG 244
Cdd:cd14160   155 SCTINMTTALHKHLW---YMPEEYIR----QGKLSVK-TDVYSFGIVIMEVLTG 200
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
43-239 3.08e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 51.20  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQgaVSLQNGKEYAVKIIEKQaghSRSRVFREVEtLYQC--QGNKNILELI----EFFEDDTRFYLVFEKLQ 116
Cdd:cd14219    13 IGKGRYGEVW--MGKWRGEKVAVKVFFTT---EEASWFRETE-IYQTvlMRHENILGFIaadiKGTGSWTQLYLITDYHE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIqKQKHFNEREASRVVRDVAAALDFLHTK--------GIAHRDLKPENILCESPEKVspvkiCDFDLGSGMKL 188
Cdd:cd14219    87 NGSLYDYL-KSTTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTC-----CIADLGLAVKF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 189 NNSCTPITTPeLTTPCGSAEYMAPEVVEVFTDQATFYDK-RCDLWSLGVVLY 239
Cdd:cd14219   161 ISDTNEVDIP-PNTRVGTKRYMPPEVLDESLNRNHFQSYiMADMYSFGLILW 211
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
36-250 3.36e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 50.97  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  36 YKLTSELlGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSR----SRVFREVetlyqcQGNKNILELIEFFEDDTRFYLV 111
Cdd:cd14128     2 YRLVRKI-GSGSFGDIYLGINITNGEEVAVKLESQKARHPQllyeSKLYKIL------QGGVGIPHIRWYGQEKDYNVLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 112 FEKLqgGSILAHIQK--QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLN 189
Cdd:cd14128    75 MDLL--GPSLEDLFNfcSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 190 NSCTPITTPELTTPCGSAEYmAPEVVEVFTDQAtfydKRCDLWSLGVVLYIMLSGYPPFVG 250
Cdd:cd14128   153 RTRQHIPYREDKNLTGTARY-ASINAHLGIEQS----RRDDMESLGYVLMYFNRGSLPWQG 208
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
142-250 3.37e-07

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 51.13  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKLNnsctpittPELTTPcGSA----EYMAPEVV-- 215
Cdd:cd05102   181 VARGMEFLASRKCIHRDLAARNILL-SENNV--VKICDFGLARDIYKD--------PDYVRK-GSArlplKWMAPESIfd 248
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 216 EVFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05102   249 KVYTTQS-------DVWSFGVLLWEIFSlGASPYPG 277
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
140-318 3.57e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 51.53  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 140 RDVAAALDFLHTKGIAHRDLKPENILCESPEKVspvkiCDFDLGSgmklnnSCTP--ITTPELTTPCGSAEYMAPEVVEv 217
Cdd:PHA03212  189 RSVLRAIQYLHENRIIHRDIKAENIFINHPGDV-----CLGDFGA------ACFPvdINANKYYGWAGTIATNAPELLA- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 218 fTDQatfYDKRCDLWSLGVVLYIMLSGYPPFVGHCG--ADCGWDRG-------------------------EVCRVCQNK 270
Cdd:PHA03212  257 -RDP---YGPAVDIWSAGIVLFEMATCHDSLFEKDGldGDCDSDRQikliirrsgthpnefpidaqanldeIYIGLAKKS 332
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 271 lfeSIQEGK-------YEFPdkdwahisSEAKDLISKLLVRDAKQRLSAAQVLQH 318
Cdd:PHA03212  333 ---SRKPGSrplwtnlYELP--------IDLEYLICKMLAFDAHHRPSAEALLDF 376
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
43-243 4.26e-07

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 50.26  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAvSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd05113    12 LGTGQFGVVKYG-KWRGQYDVAIKMI-KEGSMSEDEFIEEAKVMMNLS-HEKLVQLYGVCTKQRPIFIITEYMANGCLLN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQK-QKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLgSGMKLNNsctpittpELT 201
Cdd:cd05113    89 YLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQ---GVVKVSDFGL-SRYVLDD--------EYT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1358101401 202 TPCGS---AEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS 243
Cdd:cd05113   157 SSVGSkfpVRWSPPEVLMYSK-----FSSKSDVWAFGVLMWEVYS 196
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
104-250 4.96e-07

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 50.79  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFEKLQG-------GSILAHIQKQKHFNEREASRVVRD-----------------VAAALDFLHTKGIAHRDL 159
Cdd:cd05105   184 DTTQYVPMLEIKEAskysdiqRSNYDRPASYKGSNDSEVKNLLSDdgseglttldllsftyqVARGMEFLASKNCVHRDL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 160 KPENILCeSPEKVspVKICDFDLGSGMKLNNSCTPITTPELttpcgSAEYMAPEvvEVFTDqatFYDKRCDLWSLGVVLY 239
Cdd:cd05105   264 AARNVLL-AQGKI--VKICDFGLARDIMHDSNYVSKGSTFL-----PVKWMAPE--SIFDN---LYTTLSDVWSYGILLW 330
                         170
                  ....*....|..
gi 1358101401 240 IMLS-GYPPFVG 250
Cdd:cd05105   331 EIFSlGGTPYPG 342
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
142-250 5.11e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 50.57  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKLNnsctpittPELTTPcGSA----EYMAPEVV-- 215
Cdd:cd05054   147 VARGMEFLASRKCIHRDLAARNILL-SENNV--VKICDFGLARDIYKD--------PDYVRK-GDArlplKWMAPESIfd 214
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 216 EVFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05054   215 KVYTTQS-------DVWSFGVLLWEIFSlGASPYPG 243
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
40-239 5.50e-07

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 50.04  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKV-QGavsLQNGKEYAVKIIEKQAGHSRSrVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd05039    11 GELIGKGEFGDVmLG---DYRGQKVAVKCLKDDSTAAQA-FLAEASVMTTLR-HPNLVQLLGVVLEGNGLYIVTEYMAKG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 SIL--------AHIQKQKHFNereasrVVRDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSpvKICDFDLG--SGMKL 188
Cdd:cd05039    86 SLVdylrsrgrAVITRKDQLG------FALDVCEGMEYLESKKFVHRDLAARNVLV-SEDNVA--KVSDFGLAkeASSNQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 189 NNSCTPIttpelttpcgsaEYMAPEVVE--VFTDQAtfydkrcDLWSLGVVLY 239
Cdd:cd05039   157 DGGKLPI------------KWTAPEALRekKFSTKS-------DVWSFGILLW 190
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
43-250 5.57e-07

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 50.11  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGK----EYAVKIIEKQAGHSRSR-VFREVETLYQCqGNKNILELIEFFEDdTRFYLVFEKLQG 117
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREETGPKANEeILDEAYVMASV-DHPHLVRLLGICLS-SQVQLITQLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHI-QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLG-------SGMKLN 189
Cdd:cd05057    93 GCLLDYVrNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH---VKITDFGLAklldvdeKEYHAE 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 190 NSCTPIttpelttpcgsaEYMAPEVVE--VFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05057   170 GGKVPI------------KWMALESIQyrIYTHKS-------DVWSYGVTVWeLMTFGAKPYEG 214
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
142-246 6.10e-07

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 50.78  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENIL-CESpekvSPVKICDFDLGSG-MKLNNSctpITTPELTTPCgsaEYMAPEvvEVFT 219
Cdd:cd05107   248 VANGMEFLASKNCVHRDLAARNVLiCEG----KLVKICDFGLARDiMRDSNY---ISKGSTFLPL---KWMAPE--SIFN 315
                          90       100
                  ....*....|....*....|....*....
gi 1358101401 220 DqatFYDKRCDLWSLGVVLY--IMLSGYP 246
Cdd:cd05107   316 N---LYTTLSDVWSFGILLWeiFTLGGTP 341
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
108-239 9.30e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 49.51  E-value: 9.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 108 FYLVFEKLQGGSILAHIQKQKHfnEREASRVV---RDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGS 184
Cdd:cd05081    82 LRLVMEYLPSGCLRDFLQRHRA--RLDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVESEAH---VKIADFGLAK 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 185 GMKLNNSCTPITTPelttpcGSAE--YMAPEVVevftdQATFYDKRCDLWSLGVVLY 239
Cdd:cd05081   157 LLPLDKDYYVVREP------GQSPifWYAPESL-----SDNIFSRQSDVWSFGVVLY 202
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
43-248 9.89e-07

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 49.53  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIEkqaGHS------RSRVFREVETLYQCQGNkNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd14026     5 LSRGAFGTVSRARHADWRVTVAIKCLK---LDSpvgdseRNCLLKEAEILHKARFS-YILPILGICNEPEFLGIVTEYMT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQKHFNEREAS---RVVRDVAAALDFLH--TKGIAHRDLKPENILCESPEKvspVKICDFDLGS--GMKLN 189
Cdd:cd14026    81 NGSLNELLHEKDIYPDVAWPlrlRILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFH---VKIADFGLSKwrQLSIS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 190 NSCTPITTPElttpCGSAEYMAPEVVEvfTDQATFYDKRCDLWSLGVVLYIMLSGYPPF 248
Cdd:cd14026   158 QSRSSKSAPE----GGTIIYMPPEEYE--PSQKRRASVKHDIYSYAIIMWEVLSRKIPF 210
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
43-255 9.95e-07

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 49.27  E-value: 9.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVsLQNGKEYAVKIIekQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd05072    15 LGAGQFGEVWMGY-YNNSTKVAVKTL--KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQkhfnerEASRVV--------RDVAAALDFLHTKGIAHRDLKPENILCespEKVSPVKICDFDLGSGMKLNnsctp 194
Cdd:cd05072    92 FLKSD------EGGKVLlpklidfsAQIAEGMAYIERKNYIHRDLRAANVLV---SESLMCKIADFGLARVIEDN----- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 195 ittpELTTPCGSA---EYMAPEVVEVFTdqatfYDKRCDLWSLGVVLY-IMLSGYPPFVGHCGAD 255
Cdd:cd05072   158 ----EYTAREGAKfpiKWTAPEAINFGS-----FTIKSDVWSFGILLYeIVTYGKIPYPGMSNSD 213
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
142-250 1.23e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.59  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMKLNnsctpittPELTTPcGSA----EYMAPEVV-- 215
Cdd:cd05103   188 VAKGMEFLASRKCIHRDLAARNILL-SENNV--VKICDFGLARDIYKD--------PDYVRK-GDArlplKWMAPETIfd 255
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 216 EVFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05103   256 RVYTIQS-------DVWSFGVLLWEIFSlGASPYPG 284
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
41-250 1.96e-06

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 48.41  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKE----YAVKIIEKQAGHsrsRVFREVETLYQCQGNKN---ILELIEFFEDdTRFYLVFE 113
Cdd:cd05111    13 KVLGSGVFGTVHKGIWIPEGDSikipVAIKVIQDRSGR---QSFQAVTDHMLAIGSLDhayIVRLLGICPG-ASLQLVTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNNSc 192
Cdd:cd05111    89 LLPLGSLLDHVRQHRgSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSP---SQVQVADFGVADLLYPDDK- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 193 tPITTPELTTPCgsaEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05111   165 -KYFYSEAKTPI---KWMALESIHFGK-----YTHQSDVWSYGVTVWEMMTfGAEPYAG 214
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
41-239 2.07e-06

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 48.43  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQgavslqNGK---EYAVKIIEKQaGHSRS--RVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd14152     6 ELIGQGRWGKVH------RGRwhgEVAIRLLEID-GNNQDhlKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QGGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpekvSPVKICDFDL-------GSGMK 187
Cdd:cd14152    79 KGRTLYSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGLfgisgvvQEGRR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101401 188 LNnsctpittpELTTPCGSAEYMAPEVVEVFT-----DQATFyDKRCDLWSLGVVLY 239
Cdd:cd14152   155 EN---------ELKLPHDWLCYLAPEIVREMTpgkdeDCLPF-SKAADVYAFGTIWY 201
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
43-250 2.85e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 48.48  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKE-------YAVKIIEKQA-GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd05100    20 LGEGCFGQVVMAEAIGIDKDkpnkpvtVAVKMLKDDAtDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGGSILAHIQKQK----------------HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKIC 178
Cdd:cd05100   100 ASKGNLREYLRARRppgmdysfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED---NVMKIA 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1358101401 179 DFDLGSGMKLNNSCTPITTPELttpcgSAEYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05100   177 DFGLARDVHNIDYYKKTTNGRL-----PVKWMAPEALfdRVYTHQS-------DVWSFGVLLWeIFTLGGSPYPG 239
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
43-250 3.29e-06

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 47.81  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVsLQNGKEYAVKIIeKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSIL 121
Cdd:cd05148    14 LGSGYFGEVWEGL-WKNRVRVAIKIL-KSDDLLKQQDFqKEVQALKRLR-HKHLISLFAVCSVGEPVYIITELMEKGSLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 122 AHIQKQKHFNEREAS--RVVRDVAAALDFLHTKGIAHRDLKPENIL------CespekvspvKICDFDLGSGMKlnnscT 193
Cdd:cd05148    91 AFLRSPEGQVLPVASliDMACQVAEGMAYLEEQNSIHRDLAARNILvgedlvC---------KVADFGLARLIK-----E 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 194 PITTPELTT-PcgsAEYMAPEVVEVFTdqatfYDKRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05148   157 DVYLSSDKKiP---YKWTAPEAASHGT-----FSTKSDVWSFGILLYEMFTyGQVPYPG 207
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
41-248 3.71e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 47.56  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05065    10 EVIGAGEFGEVcRGRLKLPGKREIFVAIKTLKSGYTekqRRDFLSEASIMGQFD-HPNIIHLEGVVTKSRPVMIITEFME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHI-QKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKLNNSctpi 195
Cdd:cd05065    89 NGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSN---LVCKVSDFGLSRFLEDDTS---- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1358101401 196 tTPELTTPCGSA---EYMAPEVVEV--FTDQAtfydkrcDLWSLGVVLY-IMLSGYPPF 248
Cdd:cd05065   162 -DPTYTSSLGGKipiRWTAPEAIAYrkFTSAS-------DVWSYGIVMWeVMSYGERPY 212
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
41-251 3.72e-06

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 47.85  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGA--VSLQNGKEY---AVKIIEKQAGHSRSRVF-REVETLYQCQgNKNILELIEFFEDDTRFYLVFEK 114
Cdd:cd05049    11 RELGEGAFGKVFLGecYNLEPEQDKmlvAVKTLKDASSPDARKDFeREAELLTNLQ-HENIVKFYGVCTEGDPLLMVFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 115 LQGG--------------SILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENilCESPEKVSpVKICDF 180
Cdd:cd05049    90 MEHGdlnkflrshgpdaaFLASEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRN--CLVGTNLV-VKIGDF 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 181 dlgsGMKLNnsctpITTPELTTPCGSA----EYMAPEVV--EVFTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFVGH 251
Cdd:cd05049   167 ----GMSRD-----IYSTDYYRVGGHTmlpiRWMPPESIlyRKFTTES-------DVWSFGVVLWeIFTYGKQPWFQL 228
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
133-244 4.50e-06

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 47.49  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 133 REASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLgsgmklnnsCTP---ITTPELTTPCgsaeY 209
Cdd:cd13975   102 EERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNR---AKITDLGF---------CKPeamMSGSIVGTPI----H 165
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1358101401 210 MAPevvEVFTDQatfYDKRCDLWSLGVVLYIMLSG 244
Cdd:cd13975   166 MAP---ELFSGK---YDNSVDVYAFGILFWYLCAG 194
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
40-250 4.61e-06

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 47.37  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKV-QGAVSLQNGKEYAVKII-----EKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFE 113
Cdd:cd05048    10 LEELGEGAFGKVyKGELLGPSSEESAISVAiktlkENASPKTQQDFRREAELMSDLQ-HPNIVCLLGVCTKEQPQCMLFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 114 KLQGGSILAHIQKQKHFNEREASRVVRD----------------VAAALDFLHTKGIAHRDLKPENILcespekVSP--- 174
Cdd:cd05048    89 YMAHGDLHEFLVRHSPHSDVGVSSDDDGtassldqsdflhiaiqIAAGMEYLSSHHYVHRDLAARNCL------VGDglt 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 175 VKICDFDLGSGM-------KLNNSCTPIttpelttpcgsaEYMAPEvvevftdqATFYDK---RCDLWSLGVVLYIMLS- 243
Cdd:cd05048   163 VKISDFGLSRDIyssdyyrVQSKSLLPV------------RWMPPE--------AILYGKfttESDVWSFGVVLWEIFSy 222

                  ....*..
gi 1358101401 244 GYPPFVG 250
Cdd:cd05048   223 GLQPYYG 229
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
41-283 5.25e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 47.17  E-value: 5.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05066    10 KVIGAGEFGEVcSGRLKLPGKREIPVAIKTLKAGYTekqRRDFLSEASIMGQFD-HPNIIHLEGVVTRSKPVMIVTEYME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPekvSPVKICDFDLGSGMKlnnsctpi 195
Cdd:cd05066    89 NGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSN---LVCKVSDFGLSRVLE-------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 196 TTPE--LTTPCGS--AEYMAPEVVEV--FTDQAtfydkrcDLWSLGVVLY-IMLSGYPPFvghcgadcgWDrgevcrVCQ 268
Cdd:cd05066   158 DDPEaaYTTRGGKipIRWTAPEAIAYrkFTSAS-------DVWSYGIVMWeVMSYGERPY---------WE------MSN 215
                         250
                  ....*....|....*
gi 1358101401 269 NKLFESIQEGkYEFP 283
Cdd:cd05066   216 QDVIKAIEEG-YRLP 229
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
41-248 5.46e-06

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 47.28  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCqGNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05063    11 KVIGAGEFGEVfRGILKMPGRKEVAVAIKTLKPGYTekqRQDFLSEASIMGQF-SHHNIIRLEGVVTKFKPAMIITEYME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQ-KQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNSCTpI 195
Cdd:cd05063    90 NGALDKYLRdHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLE---CKVSDFGLSRVLEDDPEGT-Y 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101401 196 TTPELTTPCgsaEYMAPEVVEV--FTDQAtfydkrcDLWSLGVVLY-IMLSGYPPF 248
Cdd:cd05063   166 TTSGGKIPI---RWTAPEAIAYrkFTSAS-------DVWSFGIVMWeVMSFGERPY 211
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
41-248 5.62e-06

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 46.90  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQgaVSLQNGKEYAVKIIEKQAghSRSRVFREVETLYQCQgNKNILELIEFF-EDDTRFYLVFEKLQGGS 119
Cdd:cd05082    12 QTIGKGEFGDVM--LGDYRGNKVAVKCIKNDA--TAQAFLAEASVMTQLR-HSNLVQLLGVIvEEKGGLYIVTEYMAKGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 120 ILAHIqkqkhfneREASRVV----------RDVAAALDFLHTKGIAHRDLKPENILCeSPEKVSpvKICDFdlgsGMKLN 189
Cdd:cd05082    87 LVDYL--------RSRGRSVlggdcllkfsLDVCEAMEYLEGNNFVHRDLAARNVLV-SEDNVA--KVSDF----GLTKE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 NSCTPITTpelTTPcgsAEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLS-GYPPF 248
Cdd:cd05082   152 ASSTQDTG---KLP---VKWTAPEAL-----REKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
43-278 6.16e-06

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 47.06  E-value: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAvSLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd05059    12 LGSGQFGVVHLG-KWRGKIDVAIKMI-KEGSMSEDDFIEEAKVMMKLS-HPKLVQLYGVCTKQRPIFIVTEYMANGCLLN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESpEKVspVKICDFDLgSGMKLNNsctpittpELT 201
Cdd:cd05059    89 YLRERRGkFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGE-QNV--VKVSDFGL-ARYVLDD--------EYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 202 TPCGS---AEYMAPEVVevftDQATFYDKRcDLWSLGVVLYIMLS-GYPPFVghcgadcGWDRGEVcrvcqnklFESIQE 277
Cdd:cd05059   157 SSVGTkfpVKWSPPEVF----MYSKFSSKS-DVWSFGVLMWEVFSeGKMPYE-------RFSNSEV--------VEHISQ 216

                  .
gi 1358101401 278 G 278
Cdd:cd05059   217 G 217
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
104-183 7.80e-06

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 45.34  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 104 DDTRFYLVFEKLQGGSILAHIQKQKhfnerEASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEkvspVKICDFDLG 183
Cdd:COG3642    27 DPDDADLVMEYIEGETLADLLEEGE-----LPPELLRELGRLLARLHRAGIVHGDLTTSNILVDDGG----VYLIDFGLA 97
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
43-250 7.97e-06

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 46.51  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVsLQNGKEYAVKIIeKQAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQGGSILA 122
Cdd:cd05034     3 LGAGQFGEVWMGV-WNGTTKVAVKTL-KPGTMSPEAFLQEAQIMKKLR-HDKLVQLYAVCSDEEPIYIVTELMSKGSLLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 123 HIQKQKHFNEREASRV--VRDVAAALDFLHTKGIAHRDLKPENILC-ESPEkvspVKICDFDLGSGMKLNNSCT------ 193
Cdd:cd05034    80 YLRTGEGRALRLPQLIdmAAQIASGMAYLESRNYIHRDLAARNILVgENNV----CKVADFGLARLIEDDEYTAregakf 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1358101401 194 PIttpelttpcgsaEYMAPEvvevftdqATFYDK---RCDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:cd05034   156 PI------------KWTAPE--------AALYGRftiKSDVWSFGILLYeIVTYGRVPYPG 196
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
43-321 8.12e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 46.95  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKVQGAVSLQNGKEYAVKIIeKQAGHSRSRVFREVEtLYQC-------QGNKN-ILELIEFFE----DDTRFYL 110
Cdd:cd14217    20 LGWGHFSTVWLCWDMQGKRFVAMKVV-KSAQHYTETALDEIK-LLRCvresdpeDPNKDmVVQLIDDFKisgmNGIHVCM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 111 VFEKLqGGSILAHIQKQKH--FNEREASRVVRDVAAALDFLHTK-GIAHRDLKPENILC--------------------- 166
Cdd:cd14217    98 VFEVL-GHHLLKWIIKSNYqgLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvddayvrrmaaeatewqkag 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 167 ESPEKVSPVKIC-DFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEV-------VEVFTDQAtfYDKRCDLWSLGVVL 238
Cdd:cd14217   177 APPPSGSAVSTApDLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIqtrqyrsIEVLIGAG--YSTPADIWSTACMA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 239 YIMLSGYPPFVGHCGADCGWD-------------------------------RGEVCRVCQNK---LFESIQEgKYEFPD 284
Cdd:cd14217   255 FELATGDYLFEPHSGEDYSRDedhiahiiellgciprhfalsgkysreffnrRGELRHITKLKpwsLFDVLVE-KYGWPH 333
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1358101401 285 KDWAHISseakDLISKLLVRDAKQRLSAAQVLQHPWV 321
Cdd:cd14217   334 EDAAQFT----DFLIPMLEMVPEKRASAGECLRHPWL 366
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
43-250 9.26e-06

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 46.75  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV-----QGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQG 117
Cdd:cd05050    13 IGQGAFGRVfqaraPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 118 GSILAHIQKQKHFNEREASR----------------------VVRDVAAALDFLHTKGIAHRDLKPENilCESPEKVSpV 175
Cdd:cd05050    93 GDLNEFLRHRSPRAQCSLSHstssarkcglnplplscteqlcIAKQVAAGMAYLSERKFVHRDLATRN--CLVGENMV-V 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 176 KICDFDLGSGM------KLN-NSCTPIttpelttpcgsaEYMAPEvvevftdqATFYDK---RCDLWSLGVVLYIMLS-G 244
Cdd:cd05050   170 KIADFGLSRNIysadyyKASeNDAIPI------------RWMPPE--------SIFYNRyttESDVWAYGVVLWEIFSyG 229

                  ....*.
gi 1358101401 245 YPPFVG 250
Cdd:cd05050   230 MQPYYG 235
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
43-326 9.32e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 47.00  E-value: 9.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  43 LGEGAYAKV---------------QGAVSLQNGKEYAVKIIEKQA-GHSRSRVFREVETL-YQCQGNKNILELIEFFEDD 105
Cdd:PHA03210  156 LPAGAFGKIficalrasteeaearRGVNSTNQGKPKCERLIAKRVkAGSRAAIQLENEILaLGRLNHENILKIEEILRSE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 106 TRFYLVFEKLQGGSILAHIQKQKHFNER----EASRVVRDVAAALDFLHTKGIAHRDLKPENIL--CESpekvspvKICD 179
Cdd:PHA03210  236 ANTYMITQKYDFDLYSFMYDEAFDWKDRpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFlnCDG-------KIVL 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 180 FDLGSGMKLNNSCTPITTPELttpcGSAEYMAPEVVEvftdqatfYDKRC---DLWSLGVVLYIMLSGYPPFVGHCGADC 256
Cdd:PHA03210  309 GDFGTAMPFEKEREAFDYGWV----GTVATNSPEILA--------GDGYCeitDIWSCGLILLDMLSHDFCPIGDGGGKP 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 257 GWDRGEVCR---VCQN-------KLFESIQEGKYEF------PDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPW 320
Cdd:PHA03210  377 GKQLLKIIDslsVCDEefpdppcKLFDYIDSAEIDHaghsvpPLIRNLGLPADFEYPLVKMLTFDWHLRPGAAELLALPL 456

                  ....*.
gi 1358101401 321 VQGEQQ 326
Cdd:PHA03210  457 FSAEEE 462
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
142-250 9.53e-06

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 46.82  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVSpvKICDFDLGSgmKLNNSCTPITTPELTTPcgsAEYMAPEvvEVFTDQ 221
Cdd:cd05104   223 VAKGMEFLASKNCIHRDLAARNILL-THGRIT--KICDFGLAR--DIRNDSNYVVKGNARLP---VKWMAPE--SIFECV 292
                          90       100       110
                  ....*....|....*....|....*....|
gi 1358101401 222 ATFydkRCDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05104   293 YTF---ESDVWSYGILLWEIFSlGSSPYPG 319
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
41-248 1.04e-05

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 46.21  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKV-QGAVSLQNGKEYAVKIIEKQAGHS---RSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLQ 116
Cdd:cd05033    10 KVIGGGEFGEVcSGSLKLPGKKEIDVAIKTLKSGYSdkqRLDFLTEASIMGQFD-HPNVIRLEGVVTKSRPVMIVTEYME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 117 GGSILAHIQKQK-HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLGSGMKLNNsctpi 195
Cdd:cd05033    89 NGSLDKFLRENDgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLV---CKVSDFGLSRRLEDSE----- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101401 196 ttPELTTPCG--SAEYMAPEVV--EVFTdQATfydkrcDLWSLGVVLY-IMLSGYPPF 248
Cdd:cd05033   161 --ATYTTKGGkiPIRWTAPEAIayRKFT-SAS------DVWSFGIVMWeVMSYGERPY 209
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
142-250 1.08e-05

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 46.76  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 142 VAAALDFLHTKGIAHRDLKPENILCeSPEKVspVKICDFDLGSGMkLNNSCTPITtpelttpcGSA----EYMAPEVVE- 216
Cdd:cd05106   221 VAQGMDFLASKNCIHRDVAARNVLL-TDGRV--AKICDFGLARDI-MNDSNYVVK--------GNArlpvKWMAPESIFd 288
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 217 -VFTDQAtfydkrcDLWSLGVVLYIMLS-GYPPFVG 250
Cdd:cd05106   289 cVYTVQS-------DVWSYGILLWEIFSlGKSPYPG 317
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
41-319 1.14e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 46.17  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  41 ELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHS--RSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGG 118
Cdd:cd14138    11 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvdEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQNEYCNGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 119 S----ILAHIQKQKHFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILCE--SPEKVSPVKICDFDLGSG---MKLN 189
Cdd:cd14138    91 SladaISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtSIPNAASEEGDEDEWASNkviFKIG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 190 N--SCTPITTPELTTpcGSAEYMAPEVV-EVFTDQatfydKRCDLWSLGVVLyIMLSGYPPFVGHcgadcgwdrgevcrv 266
Cdd:cd14138   171 DlgHVTRVSSPQVEE--GDSRFLANEVLqENYTHL-----PKADIFALALTV-VCAAGAEPLPTN--------------- 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1358101401 267 cqNKLFESIQEGKY-EFPDKdwahISSEAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:cd14138   228 --GDQWHEIRQGKLpRIPQV----LSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
138-241 1.45e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 46.60  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 138 VVRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDF----DLGSGMKLN---NSCTPITTP--ELTTPCGSAE 208
Cdd:PLN03224  314 VMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQ---VKIIDFgaavDMCTGINFNplyGMLDPRYSPpeELVMPQSCPR 390
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1358101401 209 YMAPEVVEVFTDQATFYDkRCDL---WSLGVVLYIM 241
Cdd:PLN03224  391 APAPAMAALLSPFAWLYG-RPDLfdsYTAGVLLMQM 425
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
138-255 1.56e-05

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 45.78  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 138 VVRDVAAALDFLHTKGIAHRDLKPENILCEspEKVSpVKICDFDLGSGMK-------LNNSCTPIttpelttpcgsaEYM 210
Cdd:cd05091   130 IVTQIAAGMEYLSSHHVVHKDLATRNVLVF--DKLN-VKISDLGLFREVYaadyyklMGNSLLPI------------RWM 194
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1358101401 211 APEvvevftdqATFYDK---RCDLWSLGVVLYIMLS-GYPPFVGHCGAD 255
Cdd:cd05091   195 SPE--------AIMYGKfsiDSDIWSYGVVLWEVFSyGLQPYCGYSNQD 235
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
129-250 1.65e-05

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 46.24  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 129 HFNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekVSP---VKICDFDlgsGMKLNNsctpittPELTTPC- 204
Cdd:COG4248   117 LFDWLFLLRTARNLAAAVAALHAAGYVHGDVNPSNIL------VSDtalVTLIDTD---SFQVRD-------PGKVYRCv 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 205 -GSAEYMAPEVV-----EVFTDQATfydkrcDLWSLGVVLY-IMLSGYPPFVG 250
Cdd:COG4248   181 vGTPEFTPPELQgksfaRVDRTEEH------DRFGLAVLIFqLLMEGRHPFSG 227
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
65-239 1.76e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 45.66  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  65 VKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHfNEREAS------RV 138
Cdd:cd05042    27 VKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDLKAYLRSERE-HERGDSdtrtlqRM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 139 VRDVAAALDFLHTKGIAHRDLKPENILCESPEKvspVKICDFDLG-SGMKLNNSCTPittPELTTPCgsaEYMAPEVVEV 217
Cdd:cd05042   106 ACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLT---VKIGDYGLAhSRYKEDYIETD---DKLWFPL---RWTAPELVTE 176
                         170       180
                  ....*....|....*....|....
gi 1358101401 218 FTDQATFYD--KRCDLWSLGVVLY 239
Cdd:cd05042   177 FHDRLLVVDqtKYSNIWSLGVTLW 200
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
130-319 1.76e-05

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 44.70  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  130 FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILcespekvspvkicdfdlgsgMKLNNSCTpITTPELTTPCGSaeY 209
Cdd:smart00750  14 LNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGL--------------------LKLDGSVA-FKTPEQSRPDPY--F 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  210 MAPEVvevftDQATFYDKRCDLWSLGVVLYIMLSGYPPFVghcgadcgwdrgEVCRVCQnkLFESIQEGKYEF---PDKD 286
Cdd:smart00750  71 MAPEV-----IQGQSYTEKADIYSLGITLYEALDYELPYN------------EERELSA--ILEILLNGMPADdprDRSN 131
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1358101401  287 WAHISS--EAKDLISKLLVRDAKQRLSAAQVLQHP 319
Cdd:smart00750 132 LEGVSAarSFEDFMRLCASRLPQRREAANHYLAHC 166
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
40-249 2.26e-05

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 45.52  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401  40 SELLGEGAYAKVQGAVSLQ---NGKEYAVKIIEKQAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKL 115
Cdd:cd05043    11 SDLLQEGTFGRIFHGILRDekgKEEEVLVKTVKDHASEIQvTMLLQESSLLYGLS-HQNLLPILHVCIEDGEKPMVLYPY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 116 QG-GSILAHIQKQKHfNEREASRVVR---------DVAAALDFLHTKGIAHRDLKPENILCESpekVSPVKICDFDLGSG 185
Cdd:cd05043    90 MNwGNLKLFLQQCRL-SEANNPQALStqqlvhmalQIACGMSYLHRRGVIHKDIAARNCVIDD---ELQVKITDNALSRD 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101401 186 MKLN-------NSCTPIttpelttpcgsaEYMAPEVVevftdQATFYDKRCDLWSLGVVLYIMLS-GYPPFV 249
Cdd:cd05043   166 LFPMdyhclgdNENRPI------------KWMSLESL-----VNKEYSSASDVWSFGVLLWELMTlGQTPYV 220
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
109-255 3.28e-05

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 44.70  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101401 109 YLVFEKLQGGSILAHIQKQKH-FNEREASRVVRDVAAALDFLHTKGIAHRDLKPENILC-ESpekvSPVKICDFDLGSGM 186
Cdd:cd05068    79 YIITELMKHGSLLEYLQGKGRsLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVgEN----NICKVADFGLARVI 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101401 187 KLNNSCTpiTTPELTTPcgsAEYMAPEvvevftdqATFYDK---RCDLWSLGVVLY-IMLSGYPPFVGHCGAD 255
Cdd:cd05068   155 KVEDEYE--AREGAKFP---IKWTAPE--------AANYNRfsiKSDVWSFGILLTeIVTYGRIPYPGMTNAE 214
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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