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Conserved domains on  [gi|26051218|ref|NP_742081|]
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calcium/calmodulin-dependent protein kinase type II subunit beta isoform 8 [Homo sapiens]

Protein Classification

calcium/calmodulin-dependent protein kinase type II subunit( domain architecture ID 10197441)

calcium/calmodulin-dependent protein kinase type II (CamKII) subunit such as alpha, beta, gamma, and delta subunits, which form homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-303 0e+00

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: 659.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQ 251
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 252 MLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGA 303
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
317-444 2.86e-69

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


:

Pssm-ID: 285524  Cd Length: 128  Bit Score: 215.85  E-value: 2.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   317 RKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGED 396
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26051218   397 AACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAP 444
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-303 0e+00

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: 659.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQ 251
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 252 MLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGA 303
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-272 1.52e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 328.72  E-value: 1.52e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWfG 173
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH-KLYQQIKAGAYDFPSPEWDtVTPEAKNLINQM 252
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 26051218    253 LTINPAKRITAHEALKHPWV 272
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
14-272 1.34e-91

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 277.95  E-value: 1.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfG 173
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDED---GNLKITDFGLARQLNSGSSLT-T 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPeWDTVTPEAKNLINQML 253
Cdd:pfam00069 157 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLL 235
                         250
                  ....*....|....*....
gi 26051218   254 TINPAKRITAHEALKHPWV 272
Cdd:pfam00069 236 KKDPSKRLTATEALQHPWF 254
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
317-444 2.86e-69

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


Pssm-ID: 285524  Cd Length: 128  Bit Score: 215.85  E-value: 2.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   317 RKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGED 396
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26051218   397 AACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAP 444
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-327 1.13e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 189.57  E-value: 1.13e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLctgHEYAAKIINTKKLSARDHQKL-EREARICRLLKH-SNIVRLHDSISEEGFHYLVF 90
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERfLREIQILASLNHpPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkcKGAAVKLADFGLAIEV--- 164
Cdd:COG0515  78 EYVDGGSLedlLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR--DGRVVKLIDFGLAKLLpdp 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 ---QGDQQAWFGFAGTPGYLSPEVLR---KEAYGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQIKAGAYDFP 234
Cdd:COG0515 156 gstSSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFegekNSSATSQTLKIILELPTPSL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 235 SPEWDTVTP-----EAKNLINQMLTINPAKRITAHEALKHPWVCQRSTvasmmhRQETVECLKKFNARRKLKGAILTTML 309
Cdd:COG0515 236 ASPLSPSNPeliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKL------KESDLSDLLKPDDSAPLRLSLPPSLE 309
                       330
                ....*....|....*...
gi 26051218 310 ATRNFSARKQEIIKTTEQ 327
Cdd:COG0515 310 ALISSLNSLAISGSDLKL 327
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
13-261 2.60e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 165.76  E-value: 2.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKK-LSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   92 LVTGGELFEDI---------VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAI 162
Cdd:PTZ00263  99 FVVGGELFTHLrkagrfpndVAKFYHAE---------LVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  163 EVQgdqQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpeWdtVT 242
Cdd:PTZ00263 167 KVP---DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FD 239
                        250
                 ....*....|....*....
gi 26051218  243 PEAKNLINQMLTINPAKRI 261
Cdd:PTZ00263 240 GRARDLVKGLLQTDHTKRL 258
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-267 1.06e-25

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: 110.70  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     36 TGHEYAAKIINTKKLS-ARDHQKLEREARICRLLKHSNIVRLHDS-ISEEGFHYLVFDLVTGGELFEDIVAREYYSEADA 113
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    114 SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFG-------FAGTPGYLSPEVL 186
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVAtltrtteVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    187 RKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIkaGAYDFPSPEWDTVTPEAKnLINQMLTINPAKRITAHE 265
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQL--SPVDVSLPPWIAGHPLGQ-VLRKALNKDPRQRAASAP 238

                   ..
gi 26051218    266 AL 267
Cdd:TIGR03903  239 AL 240
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
9-214 8.02e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 107.19  E-value: 8.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    9 RFTDEYQLYEDIGKGAFSVVRR--CVKLctGHEYAAKIIntkKLS-ARDHQ---KLEREARICRLLKHSNIVRLHDSISE 82
Cdd:NF033483   4 LLGGRYEIGERIGRGGMAEVYLakDTRL--DRDVAVKVL---RPDlARDPEfvaRFRREAQSAASLSHPNIVSVYDVGED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   83 EGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI 162
Cdd:NF033483  79 GGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218  163 evqgdqqawfgfA-------------GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:NF033483 156 ------------AlssttmtqtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-303 0e+00

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: 659.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQ 251
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 252 MLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGA 303
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
14-271 1.76e-138

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: 397.23  E-value: 1.76e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWfG 173
Cdd:cd05117  82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK-T 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQML 253
Cdd:cd05117 161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLL 240
                       250
                ....*....|....*...
gi 26051218 254 TINPAKRITAHEALKHPW 271
Cdd:cd05117 241 VVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-272 1.52e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 328.72  E-value: 1.52e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWfG 173
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH-KLYQQIKAGAYDFPSPEWDtVTPEAKNLINQM 252
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 26051218    253 LTINPAKRITAHEALKHPWV 272
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
10-303 2.53e-101

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: 304.46  E-value: 2.53e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR---DHQKLEREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd14094   1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVARE----YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAI 162
Cdd:cd14094  81 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQhKLYQQIKAGAYDFPSPEWDTVT 242
Cdd:cd14094 161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHIS 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 243 PEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGA 303
Cdd:cd14094 240 ESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
14-271 4.36e-101

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: 301.74  E-value: 4.36e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAwFG 173
Cdd:cd14003  82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEFRGGSLL-KT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQM 252
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS----HLSPDARDLIRRM 233
                       250
                ....*....|....*....
gi 26051218 253 LTINPAKRITAHEALKHPW 271
Cdd:cd14003 234 LVVDPSKRITIEEILNHPW 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-271 4.98e-99

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: 296.98  E-value: 4.98e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhQKLEREARICRLLKHSNIVRLHDsISEEGFH-YLV 89
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVQLLD-IYESKSHlYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA-IEVQGDq 168
Cdd:cd14083  80 MELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSkMEDSGV- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 qawFGFA-GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd14083 159 ---MSTAcGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKD 235
                       250       260
                ....*....|....*....|....
gi 26051218 248 LINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14083 236 FIRHLMEKDPNKRYTCEQALEHPW 259
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
13-271 1.03e-93

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: 283.45  E-value: 1.03e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGdqqAW 171
Cdd:cd14095  80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSkSLKLADFGLATEVKE---PL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW--DEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLI 249
Cdd:cd14095 157 FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                       250       260
                ....*....|....*....|..
gi 26051218 250 NQMLTINPAKRITAHEALKHPW 271
Cdd:cd14095 237 SRMLVVDPEKRYSAGQVLDHPW 258
Pkinase pfam00069
Protein kinase domain;
14-272 1.34e-91

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 277.95  E-value: 1.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfG 173
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDED---GNLKITDFGLARQLNSGSSLT-T 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPeWDTVTPEAKNLINQML 253
Cdd:pfam00069 157 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLL 235
                         250
                  ....*....|....*....
gi 26051218   254 TINPAKRITAHEALKHPWV 272
Cdd:pfam00069 236 KKDPSKRLTATEALQHPWF 254
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-308 5.43e-89

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: 272.47  E-value: 5.43e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntKKLSarDHQKLEREARICRLLKHSNIVRLHDsISEEGFH-YL 88
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTV--DKKIVRTEIGVLLRLSHPNIIKLKE-IFETPTEiSL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAiEVQGDQ 168
Cdd:cd14085  76 VLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLS-KIVDQQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDE--DQHkLYQQIKAGAYDFPSPEWDTVTPEAK 246
Cdd:cd14085 155 VTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErgDQY-MFKRILNCDYDFVSPWWDDVSLNAK 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWVcqRSTVASMMHRQETVECLKKFNARRKLKGAILTTM 308
Cdd:cd14085 234 DLVKKLIVLDPKKRLTTQQALQHPWV--TGKAANFAHMDTAQKKLQEFNARRKLKAAVKAVV 293
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
10-271 3.38e-88

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: 269.61  E-value: 3.38e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKII--NTKKLSA----RDHQKLEREARICRLL-KHSNIVRLHDSISE 82
Cdd:cd14093   1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIdiTGEKSSEneaeELREATRREIEILRQVsGHPNIIELHDVFES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAI 162
Cdd:cd14093  81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VKISDFGFAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAwFGFAGTPGYLSPEVLR------KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSP 236
Cdd:cd14093 158 RLDEGEKL-RELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSP 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 237 EWDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14093 237 EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-294 4.70e-84

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: 259.54  E-value: 4.70e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIIntKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRSTGKLYALKCI--KKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAievQGDQQAWFGFA-G 176
Cdd:cd14166  87 LFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS---KMEQNGIMSTAcG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTIN 256
Cdd:cd14166 164 TPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKN 243
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26051218 257 PAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKF 294
Cdd:cd14166 244 PSKRYTCEKALSHPWIIGNTALHRDIYPSVSEQIQKNF 281
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
14-273 2.19e-83

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: 257.51  E-value: 2.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA-IEVQGdqqAWF 172
Cdd:cd14169  84 TGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLSkIEAQG---MLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQM 252
Cdd:cd14169 161 TACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHL 240
                       250       260
                ....*....|....*....|.
gi 26051218 253 LTINPAKRITAHEALKHPWVC 273
Cdd:cd14169 241 LERDPEKRFTCEQALQHPWIS 261
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-272 2.35e-81

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: 251.87  E-value: 2.35e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhQKLEREARICRLLKHSNIVRLHDsISEEGFH-YLVF 90
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDD-IYESGGHlYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAiEVQGDQQA 170
Cdd:cd14167  81 QLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLS-KIEGSGSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLIN 250
Cdd:cd14167 160 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQ 239
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWV 272
Cdd:cd14167 240 HLMEKDPEKRFTCEQALQHPWI 261
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-272 6.26e-80

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: 249.28  E-value: 6.26e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKL-CTGHEYAAKIINTKKLSARDHQKLER-----EARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKADLSSDNLKGSSRanilkEVQIMKRLSHPNIVKLLDFQESDEYY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA------SKCK----------- 149
Cdd:cd14096  82 YIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipSIVKlrkadddetkv 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 150 ---------GAA----VKLADFGLAievqgdQQAWFGFAGTP----GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYP 212
Cdd:cd14096 162 degefipgvGGGgigiVKLADFGLS------KQVWDSNTKTPcgtvGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 213 PFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14096 236 PFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
14-272 2.18e-79

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: 246.40  E-value: 2.18e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD-HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAiEVQGDQQAWF 172
Cdd:cd14081  83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADFGMA-SLQPEGSLLE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQ 251
Cdd:cd14081 159 TSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIP----HFISPDAQDLLRR 234
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14081 235 MLEVNPEKRITIEEIKKHPWF 255
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
12-271 5.30e-78

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: 243.02  E-value: 5.30e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL-IENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGdqqA 170
Cdd:cd14184  80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTkSLKLGDFGLATVVEG---P 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDED--QHKLYQQIKAGAYDFPSPEWDTVTPEAKNL 248
Cdd:cd14184 157 LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSPYWDNITDSAKEL 236
                       250       260
                ....*....|....*....|...
gi 26051218 249 INQMLTINPAKRITAHEALKHPW 271
Cdd:cd14184 237 ISHMLQVNVEARYTAEQILSHPW 259
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-280 6.36e-78

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: 244.90  E-value: 6.36e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQL---YEDIGKGAFSVVRRCVKLCTGHEYAAKIInTKKLsarDHQkleREARICRLLK-HSNIVRLHDSISEEgF 85
Cdd:cd14092   1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIV-SRRL---DTS---REVQLLRLCQgHPNIVKLHEVFQDE-L 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 H-YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA--- 161
Cdd:cd14092  73 HtYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFArlk 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFgfagTPGYLSPEVLR----KEAYGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQIKAGAYDF 233
Cdd:cd14092 153 PENQPLKTPCF----TLPYAAPEVLKqalsTQGYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSF 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 234 PSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVAS 280
Cdd:cd14092 229 DGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS 275
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
14-271 7.44e-78

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: 242.93  E-value: 7.44e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGdqqAWF 172
Cdd:cd14185  81 RGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKStTLKLADFGLAKYVTG---PIF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW--DEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLIN 250
Cdd:cd14185 158 TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRspERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLIS 237
                       250       260
                ....*....|....*....|.
gi 26051218 251 QMLTINPAKRITAHEALKHPW 271
Cdd:cd14185 238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
14-271 1.69e-77

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: 241.79  E-value: 1.69e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD-HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDmEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA-IEVQGDqqaw 171
Cdd:cd14079  84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN---VKIADFGLSnIMRDGE---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fgF----AGTPGYLSPEVLRKEAYGKP-VDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAK 246
Cdd:cd14079 157 --FlktsCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPS----HLSPGAR 230
                       250       260
                ....*....|....*....|....*
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14079 231 DLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
13-310 2.13e-77

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: 242.54  E-value: 2.13e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhqklerEARIC-RLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSE------EIEILlRYGQHPNIITLRDVYDDGNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGDQqa 170
Cdd:cd14091  75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPeSLRICDFGFAKQLRAEN-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 wfGFAGTPGY----LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYDFPSPEWDTVTP 243
Cdd:cd14091 153 --GLLMTPCYtanfVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWDHVSD 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASmmhRQetvecLKKFNARRKLKGAILTTMLA 310
Cdd:cd14091 231 SAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQ---RQ-----LTDPQDAALVKGAVAATFRA 289
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
14-271 1.40e-76

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: 239.23  E-value: 1.40e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS-ARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVArEGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd14663  82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDED---GNLKISDFGLSALSEQFRQDGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 --GFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGayDFPSPEWdtVTPEAKNLI 249
Cdd:cd14663 159 lhTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKG--EFEYPRW--FSPGAKSLI 234
                       250       260
                ....*....|....*....|..
gi 26051218 250 NQMLTINPAKRITAHEALKHPW 271
Cdd:cd14663 235 KRILDPNPSTRITVEQIMASPW 256
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
14-303 4.12e-76

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: 239.95  E-value: 4.12e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14168  12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAiEVQGDQQAWFG 173
Cdd:cd14168  91 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLS-KMEGKGDVMST 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQML 253
Cdd:cd14168 170 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDFIRNLM 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 254 TINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFnARRKLKGA 303
Cdd:cd14168 250 EKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNF-AKSKWRQA 298
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-271 1.51e-75

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: 236.26  E-value: 1.51e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR---DHQKLEReaRICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRkevEHTLNER--NILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd05123  79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL---DSDGHIKLTDFGLAKELSSDGDRTYTFCG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQMLTIN 256
Cdd:cd05123 156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFP----EYVSPEAKSLISGLLQKD 231
                       250
                ....*....|....*...
gi 26051218 257 PAKRITAH--EALK-HPW 271
Cdd:cd05123 232 PTKRLGSGgaEEIKaHPF 249
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
13-272 2.03e-75

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: 236.22  E-value: 2.03e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAw 171
Cdd:cd14007  81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHAPSNRRK- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQ 251
Cdd:cd14007 157 -TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP----SSVSPEAKDLISK 231
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14007 232 LLQKDPSKRLSLEQVLNHPWI 252
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
10-272 1.61e-73

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: 232.28  E-value: 1.61e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS------ARDHQKLEREARICRLLKHSNIVRLHDSISEE 83
Cdd:cd14084   4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTigsrreINKPRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAiE 163
Cdd:cd14084  84 DDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLS-K 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAWFGFAGTPGYLSPEVLR---KEAYGKPVDIWACGVILYILLVGYPPFWDE-DQHKLYQQIKAGAYDFPSPEWD 239
Cdd:cd14084 163 ILGETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKYTFIPKAWK 242
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 240 TVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14084 243 NVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
20-271 2.57e-73

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: 230.62  E-value: 2.57e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKklsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKR---DKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAaVKLADFGLAIEV-QGDQQawFGFAGTP 178
Cdd:cd14006  78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLnPGEEL--KEIFGTP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 179 GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPA 258
Cdd:cd14006 155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPR 234
                       250
                ....*....|...
gi 26051218 259 KRITAHEALKHPW 271
Cdd:cd14006 235 KRPTAQEALQHPW 247
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
10-271 1.37e-72

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: 229.86  E-value: 1.37e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINT--KKLSARDHQKLE----REARICRLLK-HSNIVRLHDSISE 82
Cdd:cd14181   8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVtaERLSPEQLEEVRsstlKEIHILRQVSgHPSIITLIDSYES 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAI 162
Cdd:cd14181  88 STFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLH---IKLSDFGFSC 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWfGFAGTPGYLSPEVLR------KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSP 236
Cdd:cd14181 165 HLEPGEKLR-ELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSP 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 237 EWDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14181 244 EWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
11-272 2.13e-72

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: 229.11  E-value: 2.13e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14183   5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLIEEMDMPTELYLVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGdqq 169
Cdd:cd14183  84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSkSLKLGDFGLATVVDG--- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW--DEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd14183 161 PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRgsGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKE 240
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14183 241 LITMMLQVDVDQRYSALQVLEHPWV 265
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
13-271 2.67e-72

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: 228.51  E-value: 2.67e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKK--LSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaSKCKGAAVKLADFGLAiEVQGDQQA 170
Cdd:cd14098  81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILI-TQDDPVIVKISDFGLA-KVIHTGTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKE------AYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd14098 159 LVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEE 238
                       250       260
                ....*....|....*....|....*..
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14098 239 AIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
10-274 7.11e-71

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: 225.56  E-value: 7.11e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIN---TKKLSARDHQKLeREARI--CRLLK----HSNIVRLHDSI 80
Cdd:cd14182   1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEVQEL-REATLkeIDILRkvsgHPNIIQLKDTY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGL 160
Cdd:cd14182  80 ETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN---IKLTDFGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AIEVQGDQQAwFGFAGTPGYLSPEVLR------KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFP 234
Cdd:cd14182 157 SCQLDPGEKL-REVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFG 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 26051218 235 SPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd14182 236 SPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
20-271 1.01e-70

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: 224.03  E-value: 1.01e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK--AKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWFGFaGTP 178
Cdd:cd14103  79 ERVVDDDFElTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSR-TGNQIKIIDFGLARKYDPDKKLKVLF-GTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 179 GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPA 258
Cdd:cd14103 157 EFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPR 236
                       250
                ....*....|...
gi 26051218 259 KRITAHEALKHPW 271
Cdd:cd14103 237 KRMSAAQCLQHPW 249
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
12-271 1.13e-70

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: 224.35  E-value: 1.13e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-SARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQA 170
Cdd:cd14099  81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKIGDFGLAARLEYDGER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVL-RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewDTVTPEAKNLI 249
Cdd:cd14099 158 KKTLCGTPNYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKDLI 235
                       250       260
                ....*....|....*....|..
gi 26051218 250 NQMLTINPAKRITAHEALKHPW 271
Cdd:cd14099 236 RSMLQPDPTKRPSLDEILSHPF 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
13-272 5.55e-70

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: 222.41  E-value: 5.55e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14087   2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC---RGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA-IEVQGDQQAW 171
Cdd:cd14087  79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLAsTRKKGPNCLM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQ 251
Cdd:cd14087 159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDR 238
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14087 239 LLTVNPGERLSATQALKHPWI 259
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
20-272 2.39e-69

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: 220.89  E-value: 2.39e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH------------QKLEREARICRLLKHSNIVRLHDSI--SEEGF 85
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREgkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIddPESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIE 163
Cdd:cd14008  81 LYLVLEYCEGGPVMELDSGdrVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDFGVSEM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAWFGFAGTPGYLSPEVLRKEAY---GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEwdT 240
Cdd:cd14008 158 FEDGNDTLQKTAGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPP--E 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 241 VTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14008 236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
13-271 2.79e-69

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: 220.62  E-value: 2.79e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQL-YEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsaRDHQKLEREARI-CRLLKHSNIVRLHDsISEEGFH---- 86
Cdd:cd14089   1 DYTIsKQVLGLGINGKVLECFHKKTGEKFALKVL-------RDNPKARREVELhWRASGCPHIVRIID-VYENTYQgrkc 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 -YLVFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIE 163
Cdd:cd14089  73 lLVVMECMEGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGD---QQAWFgfagTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWdeDQHKL------YQQIKAGAYDFP 234
Cdd:cd14089 153 TTTKkslQTPCY----TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY--SNHGLaispgmKKRIRNGQYEFP 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 235 SPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14089 227 NPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the ...
317-444 2.86e-69

Calcium/calmodulin dependent protein kinase II association domain; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


Pssm-ID: 285524  Cd Length: 128  Bit Score: 215.85  E-value: 2.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   317 RKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGED 396
Cdd:pfam08332   1 RKQEIIKVTETLLEAISTGDFETYTKLCDPDLTAFEPEVLGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 26051218   397 AACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAP 444
Cdd:pfam08332  81 SACIAYVRLTTYLDKNGKAHTRQSEETRVWHKRDGKWQIVHVHRSAAP 128
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
12-272 7.24e-68

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: 217.35  E-value: 7.24e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR----DHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14105   5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvSREDIEREVSILRQVLHPNIITLHDVFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKC-KGAAVKLADFGLAIEVQg 166
Cdd:cd14105  85 LILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvPIPRIKLIDFGLAHKIE- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAK 246
Cdd:cd14105 164 DGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSELAK 243
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14105 244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
14-272 3.58e-66

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: 212.63  E-value: 3.58e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSArDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGD-DLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQ-GDQQAWF 172
Cdd:cd14078  84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN---LKLIDFGLCAKPKgGMDHHLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfpSPEWdtVTPEAKNLINQ 251
Cdd:cd14078 161 TCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE--EPEW--LSPSSKLLLDQ 236
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14078 237 MLQVDPKKRITVKELLNHPWV 257
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
12-272 1.29e-65

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: 211.42  E-value: 1.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKLSARDHQKLEREAR----ICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKTTG-----KLYTCKKFLKRDGRKVRKAAKneinILKMVKHPNILQLVDVFETRKEYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA-IEVQG 166
Cdd:cd14088  76 IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAkLENGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAwfgfAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDE------DQH--KLYQQIKAGAYDFPSPEW 238
Cdd:cd14088 156 IKEP----CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEaeeddyENHdkNLFRKILAGDYEFDSPYW 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 239 DTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14088 232 DDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
6-272 6.23e-65

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: 209.90  E-value: 6.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   6 TCTRFTDEYQL-YEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLK-HSNIVRLHDSISEE 83
Cdd:cd14106   1 STENINEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKdCPRVVNLHEVYETR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIE 163
Cdd:cd14106  81 SELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTP 243
Cdd:cd14106 161 IGEGEEI-REILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSP 239
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14106 240 LAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
10-310 6.30e-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: 207.94  E-value: 6.30e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQklEREARICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd14178   1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK---RDPS--EEIEILLRYGQHPNIITLKDVYDDGKFVYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGDQ 168
Cdd:cd14178  76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPeSIRICDFGFAKQLRAEN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 qawfGFAGTPGY----LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYDFPSPEWDTV 241
Cdd:cd14178 156 ----GLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSI 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVA-SMMHRQETveclkkfnarRKLKGAILTTMLA 310
Cdd:cd14178 232 SDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSqNQLSRQDV----------HLVKGAMAATYFA 291
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
12-272 4.39e-63

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: 205.73  E-value: 4.39e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDI-GKGAFSVVRRCVKLCTGHEYAAKIINtkKLSARDHQKLEREARI---CRllKHSNIVRLHDSISEEGFHY 87
Cdd:cd14090   1 DLYKLTGELlGEGAYASVQTCINLYTGKEYAVKIIE--KHPGHSRSRVFREVETlhqCQ--GHPNILQLIEYFEDDERFY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGD 167
Cdd:cd14090  77 LVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKLS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFA--------GTPGYLSPEVLRK---EA--YGKPVDIWACGVILYILLVGYPPF---------WDED------Q 219
Cdd:cd14090 157 STSMTPVTtpelltpvGSAEYMAPEVVDAfvgEAlsYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgWDRGeacqdcQ 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 26051218 220 HKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14090 237 ELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
14-272 1.23e-62

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: 203.33  E-value: 1.23e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA--IEVQGDQQAW 171
Cdd:cd14069  83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEN---DNLKISDFGLAtvFRYKGKERLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPfWDE--DQHKLYQQIKAGAYDFPSPeWDTVTPEAKNL 248
Cdd:cd14069 160 NKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELP-WDQpsDSCQEYSDWKENKKTYLTP-WKKIDTAALSL 237
                       250       260
                ....*....|....*....|....
gi 26051218 249 INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14069 238 LRKILTENPNKRITIEDIKKHPWY 261
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
11-272 1.68e-62

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: 204.23  E-value: 1.68e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLY--EDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsaRDHQKLEREARICRLLK-HSNIVRLHD----SISEE 83
Cdd:cd14171   3 LEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCSgHPNIVQIYDvyanSVQFP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHY------LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLAD 157
Cdd:cd14171  76 GESSprarllIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLAIEVQGD-QQAWFgfagTPGYLSPEVL------RKE-----------AYGKPVDIWACGVILYILLVGYPPFWDEDQ 219
Cdd:cd14171 156 FGFAKVDQGDlMTPQF----TPYYVAPQVLeaqrrhRKErsgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 220 HK-----LYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14171 232 SRtitkdMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
9-310 1.89e-62

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: 204.09  E-value: 1.89e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQklEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd14177   1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK---RDPS--EEIEILMRYGQHPNIITLKDVYDDGRYVYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGD 167
Cdd:cd14177  76 VTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFAKQLRGE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd14177 156 NGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPWVCQRStvaSMMHRQetvecLKKFNARRKLKGAILTTMLA 310
Cdd:cd14177 236 AKDLLSHMLHVDPHQRYTAEQVLKHSWIACRD---QLPHYQ-----LNRQDAPHLVKGAMAATYSA 293
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
14-272 2.97e-62

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: 202.41  E-value: 2.97e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRC--VKLCTGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKfLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd14080  82 EYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL---DSNNNVKLSDFGFARLCPDDDGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFG--FAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLY-QQIKAGAYdFPSPEWDtVTPEAK 246
Cdd:cd14080 159 VLSktFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLkDQQNRKVR-FPSSVKK-LSPECK 236
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14080 237 DLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
12-272 4.88e-62

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: 202.04  E-value: 4.88e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSarDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14114   2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHES--DKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd14114  80 FLSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTK-RSNEVKLIDFGLATHLDPKESV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGfAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLIN 250
Cdd:cd14114 159 KVT-TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIR 237
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWV 272
Cdd:cd14114 238 KLLLADPNKRMTIHQALEHPWL 259
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
12-286 6.79e-62

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: 202.56  E-value: 6.79e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQklEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14175   1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK---RDPS--EEIEILLRYGQHPNIITLKDVYDDGKHVYLVTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGDQqa 170
Cdd:cd14175  76 LMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPeSLRICDFGFAKQLRAEN-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 wfGFAGTPGY----LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWD---EDQHKLYQQIKAGAYDFPSPEWDTVTP 243
Cdd:cd14175 154 --GLLMTPCYtanfVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKFTLSGGNWNTVSD 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVA-SMMHRQE 286
Cdd:cd14175 232 AAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPqSQLNHQD 275
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
9-315 2.09e-61

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: 202.94  E-value: 2.09e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDhqKLEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd14176  16 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RD--PTEEIEILLRYGQHPNIITLKDVYDDGKYVYV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEVQGD 167
Cdd:cd14176  91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPeSIRICDFGFAKQLRAE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd14176 171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDT 250
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPWVCQRSTVAS-MMHRQEtveclkkfnARRKLKGAILTTMLA-TRNFS 315
Cdd:cd14176 251 AKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQyQLNRQD---------APHLVKGAMAATYSAlNRNQS 314
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
14-268 7.89e-61

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: 198.58  E-value: 7.89e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS-ARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd14014  82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL---TEDGRVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 G-FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQ 251
Cdd:cd14014 159 GsVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238
                       250
                ....*....|....*..
gi 26051218 252 MLTINPAKRITAHEALK 268
Cdd:cd14014 239 ALAKDPEERPQSAAELL 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
12-272 8.05e-61

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: 199.07  E-value: 8.05e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR----DHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14195   5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvSREEIEREVNILREIQHPNIITLHDIFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-CKGAAVKLADFGLAIEVQG 166
Cdd:cd14195  85 LILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKnVPNPRIKLIDFGIAHKIEA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQaWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAK 246
Cdd:cd14195 165 GNE-FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAK 243
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14195 244 DFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
14-270 1.06e-60

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: 198.46  E-value: 1.06e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd08215  82 DGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFL---TKDGVVKLGDFGISKVLESTTD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPSPEwdTVTPEAKNLI 249
Cdd:cd08215 159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYP-PIPS--QYSSELRDLV 235
                       250       260
                ....*....|....*....|.
gi 26051218 250 NQMLTINPAKRITAHEALKHP 270
Cdd:cd08215 236 NSMLQKDPEKRPSANEILSSP 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
20-270 1.97e-60

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: 196.34  E-value: 1.97e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIP-KEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAG-- 176
Cdd:cd00180  80 DLLKENKGPlSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDSDDSLLKTTGGtt 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILlvgyppfwdedqhklyqqikagaydfpspewdtvtPEAKNLINQMLTIN 256
Cdd:cd00180 157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYD 201
                       250
                ....*....|....
gi 26051218 257 PAKRITAHEALKHP 270
Cdd:cd00180 202 PKKRPSAKELLEHL 215
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
20-271 2.37e-60

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: 197.06  E-value: 2.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAwFGFAGTPG 179
Cdd:cd14009  81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMA-ETLCGSPL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 180 YLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAK 259
Cdd:cd14009 160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                       250
                ....*....|..
gi 26051218 260 RITAHEALKHPW 271
Cdd:cd14009 240 RISFEEFFAHPF 251
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-280 3.24e-60

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: 199.11  E-value: 3.24e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYE------DIGKGAFSVVRRCVKLCTGHEYAAKIIntkklSARDHQKLEREARICRLLK-HSNIVRLHDSISEEGFH 86
Cdd:cd14179   3 YQHYEldlkdkPLGEGSFSICRKCLHKKTNQEYAVKIV-----SKRMEANTQREIAALKLCEgHPNIVKLHEVYHDQLHT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQG 166
Cdd:cd14179  78 FLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH-------KLYQQIKAGAYDFPSPEWD 239
Cdd:cd14179 158 DNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWK 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26051218 240 TVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVAS 280
Cdd:cd14179 238 NVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSS 278
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
12-272 3.64e-60

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: 197.49  E-value: 3.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR----DHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14196   5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-CKGAAVKLADFGLAIEVQg 166
Cdd:cd14196  85 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnIPIPHIKLIDFGLAHEIE- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAK 246
Cdd:cd14196 164 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSELAK 243
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14196 244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
14-272 2.35e-59

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: 195.07  E-value: 2.35e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLhdsisEEGFH-----YL 88
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHL-----EEVFEtpkrmYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAA----VKLADFGLAIEV 164
Cdd:cd14097  78 VMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSVQK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWF-GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTP 243
Cdd:cd14097 158 YGLGEDMLqETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSD 237
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14097 238 AAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
12-272 3.00e-59

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: 195.63  E-value: 3.00e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDI-GKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARI---CRllKHSNIVRLHDSISEEGFHY 87
Cdd:cd14173   1 DVYQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKRPGHSR--SRVFREVEMlyqCQ--GHRNVLELIEFFEEEDKFY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADF--GLAIEVQ 165
Cdd:cd14173  77 LVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGSGIKLN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQA-----WFGFAGTPGYLSPEVLR---KEA--YGKPVDIWACGVILYILLVGYPPF---------WDED------QH 220
Cdd:cd14173 157 SDCSPistpeLLTPCGSAEYMAPEVVEafnEEAsiYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgWDRGeacpacQN 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 221 KLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14173 237 MLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
12-272 5.33e-59

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: 194.47  E-value: 5.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-SAR---DHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14194   5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkSSRrgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-CKGAAVKLADFGLA--IEV 164
Cdd:cd14194  85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnVPKPRIKIIDFGLAhkIDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGfagTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd14194 165 GNEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSAL 241
                       250       260
                ....*....|....*....|....*...
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14194 242 AKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
13-272 1.29e-58

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: 192.80  E-value: 1.29e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVV--RRCVKlcTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05122   1 LFEILEKIGKGGFGVVykARHKK--TGQIVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELfEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQ 168
Cdd:cd05122  77 EFCSGGSL-KDLLknTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE---VKLIDFGLSAQLSDGK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI-KAGAYDFPSPEWdtVTPEAKN 247
Cdd:cd05122 153 TR-NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIaTNGPPGLRNPKK--WSKEFKD 229
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd05122 230 FLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
20-271 8.45e-58

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: 191.28  E-value: 8.45e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQ---KLEREarICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVdsvLAERN--ILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGL----AIEVQGDQQAWF 172
Cdd:cd05579  79 DLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN---GHLKLTDFGLskvgLVRRQIKLSIQK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 -----------GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFpsPEWDTV 241
Cdd:cd05579 156 ksngapekedrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEW--PEDPEV 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 242 TPEAKNLINQMLTINPAKRI---TAHEALKHPW 271
Cdd:cd05579 234 SDEAKDLISKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
12-271 9.98e-58

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: 191.27  E-value: 9.98e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTK---KLSARDHQKLEREArICRLlKHSNIVRLHDSISEEGFHYL 88
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiiKEKKVKYVTIEKEV-LSRL-AHPGIVKLYYTFQDESKLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA------- 161
Cdd:cd05581  79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTAkvlgpds 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFG----------FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAY 231
Cdd:cd05581 156 SPESTKGDADSQiaynqaraasFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEY 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 26051218 232 DFPspewDTVTPEAKNLINQMLTINPAKRITAHE-----ALK-HPW 271
Cdd:cd05581 236 EFP----ENFPPDAKDLIQKLLVLDPSKRLGVNEnggydELKaHPF 277
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
14-272 1.61e-57

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: 189.91  E-value: 1.61e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR-DHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAiEVQGDQQAWF 172
Cdd:cd14073  83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGLS-NLYSKDKLLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDtvtpeAKNLINQ 251
Cdd:cd14073 159 TFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSD-----ASGLIRW 233
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14073 234 MLTVNPKRRATIEDIANHWWV 254
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
14-272 4.18e-57

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: 188.88  E-value: 4.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAwFG 173
Cdd:cd14072  82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDAD---MNIKIADFGFSNEFTPGNKL-DT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAYGKP-VDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQM 252
Cdd:cd14072 158 FCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF----YMSTDCENLLKKF 233
                       250       260
                ....*....|....*....|
gi 26051218 253 LTINPAKRITAHEALKHPWV 272
Cdd:cd14072 234 LVLNPSKRGTLEQIMKDRWM 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
18-272 2.19e-56

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: 187.43  E-value: 2.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14193  10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKAR--SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWFGFaG 176
Cdd:cd14193  88 LFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSR-EANQVKIIDFGLARRYKPREKLRVNF-G 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTIN 256
Cdd:cd14193 166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKE 245
                       250
                ....*....|....*.
gi 26051218 257 PAKRITAHEALKHPWV 272
Cdd:cd14193 246 KSWRMSASEALKHPWL 261
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
14-271 1.03e-55

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: 185.29  E-value: 1.03e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQ--QAW 171
Cdd:cd14071  82 SNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN---IKIADFGFSNFFKPGEllKTW 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fgfAGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLIN 250
Cdd:cd14071 159 ---CGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPF----FMSTDCEHLIR 231
                       250       260
                ....*....|....*....|.
gi 26051218 251 QMLTINPAKRITAHEALKHPW 271
Cdd:cd14071 232 RMLVLDPSKRLTIEQIKKHKW 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-327 1.13e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 189.57  E-value: 1.13e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLctgHEYAAKIINTKKLSARDHQKL-EREARICRLLKH-SNIVRLHDSISEEGFHYLVF 90
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERfLREIQILASLNHpPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkcKGAAVKLADFGLAIEV--- 164
Cdd:COG0515  78 EYVDGGSLedlLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR--DGRVVKLIDFGLAKLLpdp 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 ---QGDQQAWFGFAGTPGYLSPEVLR---KEAYGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQIKAGAYDFP 234
Cdd:COG0515 156 gstSSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFegekNSSATSQTLKIILELPTPSL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 235 SPEWDTVTP-----EAKNLINQMLTINPAKRITAHEALKHPWVCQRSTvasmmhRQETVECLKKFNARRKLKGAILTTML 309
Cdd:COG0515 236 ASPLSPSNPeliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKL------KESDLSDLLKPDDSAPLRLSLPPSLE 309
                       330
                ....*....|....*...
gi 26051218 310 ATRNFSARKQEIIKTTEQ 327
Cdd:COG0515 310 ALISSLNSLAISGSDLKL 327
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
14-271 2.52e-55

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: 183.98  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLK----HSNIVRLHDSISEEGF-H-Y 87
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDF---RHPKAALREIKLLKHLNdvegHPNIVKLLDVFEHRGGnHlC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVtGGELFEdiVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAieV 164
Cdd:cd05118  78 LVFELM-GMNLYE--LIKDYprgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADFGLA--R 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPF--WDEDQHKLYQQIKAGaydfpspewdtv 241
Cdd:cd05118 151 SFTSPPYTPYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFpgDSEVDQLAKIVRLLG------------ 218
                       250       260       270
                ....*....|....*....|....*....|
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd05118 219 TPEALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
12-272 7.90e-55

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: 184.08  E-value: 7.90e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDI-GKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREArICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14174   1 DLYRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVET-LYQCQGNKNILELIEFFEDDTRFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd14174  80 EKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSAC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 -------WFGFAGTPGYLSPEVLR---KEA--YGKPVDIWACGVILYILLVGYPPF---------WDED------QHKLY 223
Cdd:cd14174 160 tpittpeLTTPCGSAEYMAPEVVEvftDEAtfYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgWDRGevcrvcQNKLF 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 224 QQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14174 240 ESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
12-271 1.12e-54

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: 183.55  E-value: 1.12e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKK---LSARDHQKLEReaRICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQVEHVLNEK--RILSEVRHPFIVNLLGSFQDDRNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVqgDQ 168
Cdd:cd05580  79 VMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL---DSDGHIKITDFGFAKRV--KD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewdtVTPEAKNL 248
Cdd:cd05580 154 RTY-TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSF----FDPDAKDL 228
                       250       260
                ....*....|....*....|....*...
gi 26051218 249 INQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05580 229 IKRLLVVDLTKRLgnlknGVEDIKNHPW 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-280 2.70e-54

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: 183.53  E-value: 2.70e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYE------DIGKGAFSVVRRCVKLCTGHEYAAKIIntkklSARDHQKLEREARICRLLK-HSNIVRLHDSISEEGFH 86
Cdd:cd14180   2 FQCYEldleepALGEGSFSVCRKCRHRQSGQEYAVKII-----SRRMEANTQREVAALRLCQsHPNIVALHEVLHDQYHT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA-IEVQ 165
Cdd:cd14180  77 YLVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFArLRPQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GD---QQAWFgfagTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH-------KLYQQIKAGAYDFPS 235
Cdd:cd14180 157 GSrplQTPCF----TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEG 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 26051218 236 PEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVAS 280
Cdd:cd14180 233 EAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSS 277
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
20-272 4.80e-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: 181.18  E-value: 4.80e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:cd06606   8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSL- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAReyY---SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFG--F 174
Cdd:cd06606  87 ASLLKK--FgklPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV---VKLADFGCAKRLAEIATGEGTksL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHklYQQIKAGAYDFPSPEW-DTVTPEAKNLINQML 253
Cdd:cd06606 162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNP--VAALFKIGSSGEPPPIpEHLSEEAKDFLRKCL 239
                       250
                ....*....|....*....
gi 26051218 254 TINPAKRITAHEALKHPWV 272
Cdd:cd06606 240 QRDPKKRPTADELLQHPFL 258
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
14-272 6.87e-54

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: 180.69  E-value: 6.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS--ARDHqkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDdvSKAH--LFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLADFGLAIEVQGDQQA 170
Cdd:cd14074  83 LGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG--LVKLTDFGFSNKFQPGEKL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 wFGFAGTPGYLSPEVLRKEAYGKP-VDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLI 249
Cdd:cd14074 161 -ETSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP----AHVSPECKDLI 235
                       250       260
                ....*....|....*....|...
gi 26051218 250 NQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14074 236 RRMLIRDPKKRASLEEIENHPWL 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
14-272 2.58e-53

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: 179.07  E-value: 2.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDqQAWFG 173
Cdd:cd14075  84 SGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN---NCVKVGDFGFSTHAKRG-ETLNT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQM 252
Cdd:cd14075 160 FCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP----SYVSEPCQELIRGI 235
                       250       260
                ....*....|....*....|
gi 26051218 253 LTINPAKRITAHEALKHPWV 272
Cdd:cd14075 236 LQPVPSDRYSIDEIKNSEWL 255
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
11-272 2.91e-53

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: 179.41  E-value: 2.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDI-GKGAFSVVRRCVKLCTGHEYAAKIIntkklsaRDHQKLEREARI-CRLLKHSNIVRLHDsISEEGFH-- 86
Cdd:cd14172   2 TDDYKLSKQVlGLGVNGKVLECFHRRTGQKCALKLL-------YDSPKARREVEHhWRASGGPHIVHILD-VYENMHHgk 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 ---YLVFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA 161
Cdd:cd14172  74 rclLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK----LYQQIKAGAYDFPSPE 237
Cdd:cd14172 154 KETT-VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAispgMKRRIRMGQYGFPNPE 232
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 238 WDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14172 233 WAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
14-272 3.93e-53

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: 179.18  E-value: 3.93e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIN--TKKLSARDHQKLE-----------REARICRLLKHSNIVRLHDSI 80
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPraSNAGLKKEREKRLekeisrdirtiREAALSSLLNHPHICRLRDFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGL 160
Cdd:cd14077  83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS---KSGNIKIIDFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AiEVQGDQQAWFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewd 239
Cdd:cd14077 160 S-NLYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPS---- 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 240 TVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14077 235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
20-271 8.32e-53

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: 177.80  E-value: 8.32e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSvvrrCVKLC----TGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05572   1 LGVGGFG----RVELVqlksKGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfGF 174
Cdd:cd05572  77 GGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN---GYVKLVDFGFAKKLGSGRKTW-TF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW--DEDQHKLYQQIKAG--AYDFPSpewdTVTPEAKNLIN 250
Cdd:cd05572 153 CGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKGidKIEFPK----YIDKNAKNLIK 228
                       250       260
                ....*....|....*....|....*.
gi 26051218 251 QMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05572 229 QLLRRNPEERLgylkgGIRDIKKHKW 254
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
12-271 2.50e-52

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: 179.40  E-value: 2.50e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARicRLLKHSN---IVRLHDSISEEGFHYL 88
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAER--DILADADspwIVRLHYAFQDEDHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGEL---------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFG 159
Cdd:cd05573  79 VMEYMPGGDLmnllikydvFPEETARFYIAE---------LVLALDSLHKLGFIHRDIKPDNILLDAD---GHIKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 160 LAIEVQGDQQAWFGF-----------------------------AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVG 210
Cdd:cd05573 147 LCTKMNKSGDRESYLndsvntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYG 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 211 YPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTiNPAKRIT-AHEALKHPW 271
Cdd:cd05573 227 FPPFYSDSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLC-DPEDRLGsAEEIKAHPF 287
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
14-272 3.52e-52

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: 176.33  E-value: 3.52e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRR--CVKLctGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKaySTKH--KCKVAIKIVSKKKAPEDYLQKfLPREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd14162  80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD---KNNNLKITDFGFARGVMKTKDG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WF----GFAGTPGYLSPEVLRKEAYgKPV--DIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYdFPSPEwdTVTPE 244
Cdd:cd14162 157 KPklseTYCGSYAYASPEILRGIPY-DPFlsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVV-FPKNP--TVSEE 232
                       250       260
                ....*....|....*....|....*....
gi 26051218 245 AKNLINQMLTinPAK-RITAHEALKHPWV 272
Cdd:cd14162 233 CKDLILRMLS--PVKkRITIEEIKRDPWF 259
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
11-272 1.40e-51

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: 174.72  E-value: 1.40e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLY--EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd14190   1 SSTFSIHskEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ--NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGD 167
Cdd:cd14190  79 FMEYVEGGELFERIVDEDYHlTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNR-TGHQVKIIDFGLARRYNPR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFaGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd14190 158 EKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKD 236
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14190 237 FVSNLIIKERSARMSATQCLKHPWL 261
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
20-272 1.81e-51

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: 174.42  E-value: 1.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHE--YAAKIINTKKLSARDHQ---KLEREARICRLLKHSNIVRLHDSISEEGFHY-LVFDLV 93
Cdd:cd13994   1 IGKGATSVVRIVTKKNPRSGvlYAVKEYRRRDDESKRKDyvkRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLA--IEVQGDQQA- 170
Cdd:cd13994  81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG---VLKLTDFGTAevFGMPAEKESp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 -WFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd13994 158 mSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLLPSE 237
                       250       260
                ....*....|....*....|....*...
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd13994 238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
13-272 2.93e-50

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: 171.51  E-value: 2.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKL-----CTGHEYAAKIINTKKLSARDHQ-KLEREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd14076   2 PYILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRDTQQENCQTsKIMREINILKGLTHPNIVRLLDVLKTKKYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQG 166
Cdd:cd14076  82 GIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD---KNRNLVITDFGFANTFDH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFA-GTPGYLSPE-VLRKEAY-GKPVDIWACGVILYILLVGYPPfWDEDQH--------KLYQQIKAGAYDFPs 235
Cdd:cd14076 159 FNGDLMSTScGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLP-FDDDPHnpngdnvpRLYRYICNTPLIFP- 236
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 236 pewDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14076 237 ---EYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
19-272 3.64e-50

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: 171.39  E-value: 3.64e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVrrcvKLCTGHE----YAAKIINTKKL-------------------SARDH--QKLEREARICRLLKHSNI 73
Cdd:cd14118   1 EIGKGSYGIV----KLAYNEEdntlYAMKILSKKKLlkqagffrrppprrkpgalGKPLDplDRVYREIAILKKLDHPNV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  74 VRLHDSISE--EGFHYLVFDLVTGGELFEDIvAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskCKGA 151
Cdd:cd14118  77 VKLVEVLDDpnEDNLYMVFELVDKGAVMEVP-TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG--DDGH 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 152 aVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKA 228
Cdd:cd14118 154 -VKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 26051218 229 GAYDFpsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14118 233 DPVVF--PDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
13-272 4.02e-50

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: 170.48  E-value: 4.02e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd06627  81 VENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTT---KDGLVKLADFGVATKLNEVEKDEN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWD-----------EDQHKlyqqikagaydfPSPEwdTV 241
Cdd:cd06627 158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDlqpmaalfrivQDDHP------------PLPE--NI 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06627 224 SPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
11-272 1.81e-49

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: 169.03  E-value: 1.81e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14191   1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLA--IEVQGD 167
Cdd:cd14191  79 EMVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTKIKLIDFGLArrLENAGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGfagTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd14191 158 LKVLFG---TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKD 234
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14191 235 FISNLLKKDMKARLTCTQCLQHPWL 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
12-272 1.95e-49

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: 168.97  E-value: 1.95e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd14002  81 YAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCNTLVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQ 251
Cdd:cd14002 157 TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWP----SNMSPEFKSFLQG 232
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd14002 233 LLNKDPSKRLSWPDLLEHPFV 253
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
17-272 2.41e-49

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: 168.99  E-value: 2.41e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14192   9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVK--GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWFGFa 175
Cdd:cd14192  87 ELFDRITDESYQlTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNS-TGNQIKIIDFGLARRYKPREKLKVNF- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTI 255
Cdd:cd14192 165 GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVK 244
                       250
                ....*....|....*..
gi 26051218 256 NPAKRITAHEALKHPWV 272
Cdd:cd14192 245 EKSCRMSATQCLKHEWL 261
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-271 7.59e-49

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: 168.38  E-value: 7.59e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIN-TKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAiPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQgdQQA 170
Cdd:cd05612  81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLD---KEGHIKLTDFGFAKKLR--DRT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLIN 250
Cdd:cd05612 156 W-TLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR----HLDLYAKDLIK 230
                       250       260
                ....*....|....*....|....*.
gi 26051218 251 QMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05612 231 KLLVVDRTRRLgnmknGADDVKNHRW 256
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
14-272 1.20e-48

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: 167.05  E-value: 1.20e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKlCTGHEYAAKIINTKKLsaRDHQKL---EREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRI--KDEQDLlhiRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGaAVKLADFGLAIEVQGDQ-- 168
Cdd:cd14161  82 EYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL--DANG-NIKIADFGLSNLYNQDKfl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAwfgFAGTPGYLSPEVLRKEAYGKP-VDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDtvtpeAKN 247
Cdd:cd14161 159 QT---YCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSD-----ACG 230
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14161 231 LIRWLLMVNPERRATLEDVASHWWV 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-270 2.27e-48

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: 166.56  E-value: 2.27e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFH--YLVF 90
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTtlYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCH-----QMGVVHRDLKPENLLLaskCKGAAVKLADFGLA 161
Cdd:cd08217  81 EYCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFL---DSDNNVKLGDFGLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPSPewDTV 241
Cdd:cd08217 158 RVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFP-RIP--SRY 234
                       250       260
                ....*....|....*....|....*....
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd08217 235 SSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
14-271 2.66e-48

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: 165.93  E-value: 2.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGE---KIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWfG 173
Cdd:cd14665  79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGS-PAPRLKICDFGYSKSSVLHSQPK-S 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLY----QQIKAGAYDFpsPEWDTVTPEAKNL 248
Cdd:cd14665 157 TVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFrktiQRILSVQYSI--PDYVHISPECRHL 234
                       250       260
                ....*....|....*....|...
gi 26051218 249 INQMLTINPAKRITAHEALKHPW 271
Cdd:cd14665 235 ISRIFVADPATRITIPEIRNHEW 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
14-271 5.07e-48

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: 166.12  E-value: 5.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsardhqKLE-----------REARICRLLKHSNIVRLHDSISE 82
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI-----------RLDneeegipstalREISLLKELKHPNIVKLLDVIHT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDlvtggelfedivareyYSEADASHCI----------------QQILEAVLHCHQMGVVHRDLKPENLLLAS 146
Cdd:cd07829  70 ENKLYLVFE----------------YCDQDLKKYLdkrpgplppnliksimYQLLRGLAYCHSHRILHRDLKPQNLLINR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 147 KCKgaaVKLADFGLAIEvqgdqqawFGFAG--------TPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVGYPPFW-D 216
Cdd:cd07829 134 DGV---LKLADFGLARA--------FGIPLrtythevvTLWYRAPEILLGSkHYSTAVDIWSVGCIFAELITGKPLFPgD 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 217 EDQHKLYQ--QI-------------KAGAYDFPSPEWD---------TVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07829 203 SEIDQLFKifQIlgtpteeswpgvtKLPDYKPTFPKWPkndlekvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-272 6.41e-48

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: 165.49  E-value: 6.41e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLY--EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN-IVRLHDSISEEGFH 86
Cdd:cd14197   5 FQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPwVINLHEVYETASEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEV 164
Cdd:cd14197  85 ILVLEYAAGGEIFNQCVAdrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRIL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPE 244
Cdd:cd14197 165 KNSEELR-EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSES 243
                       250       260
                ....*....|....*....|....*...
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14197 244 AIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
14-271 9.08e-48

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: 164.51  E-value: 9.08e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYED--IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14082   3 YQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGgELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAiEVQGDQQ 169
Cdd:cd14082  83 KLHG-DMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFA-RIIGEKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFwDEDQhKLYQQIKAGAYDFPSPEWDTVTPEAKNLI 249
Cdd:cd14082 161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDE-DINDQIQNAAFMYPPNPWKEISPDAIDLI 238
                       250       260
                ....*....|....*....|..
gi 26051218 250 NQMLTINPAKRITAHEALKHPW 271
Cdd:cd14082 239 NNLLQVKMRKRYSVDKSLSHPW 260
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
14-271 9.40e-48

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: 164.35  E-value: 9.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSvRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAwF 172
Cdd:cd05578  82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQ---GHVHITDFNIATKLTDGTLA-T 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW-------DEDQHKLYQQIKagayDFPsPEWDTvtpEA 245
Cdd:cd05578 158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEihsrtsiEEIRAKFETASV----LYP-AGWSE---EA 229
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALK-HPW 271
Cdd:cd05578 230 IDLINKLLERDPQKRLGDLSDLKnHPY 256
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
12-278 1.00e-47

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: 165.98  E-value: 1.00e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDI-GKGAFSVVRRCVKLCTGHEYAAKIIntkklsaRDHQKLEREARI-CRLLKHSNIVRLHDsISEEGFH--- 86
Cdd:cd14170   1 DDYKVTSQVlGLGINGKVLQIFNKRTQEKFALKML-------QDCPKARREVELhWRASQCPHIVRIVD-VYENLYAgrk 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 --YLVFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAI 162
Cdd:cd14170  73 clLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDED----QHKLYQQIKAGAYDFPSPEW 238
Cdd:cd14170 153 ETT-SHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEW 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 26051218 239 DTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTV 278
Cdd:cd14170 232 SEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKV 271
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
12-272 1.51e-47

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: 163.88  E-value: 1.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-SARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMqKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQ 169
Cdd:cd14186  81 EMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN---IKIADFGLATQLKMPHE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLI 249
Cdd:cd14186 158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMP----AFLSREAQDLI 233
                       250       260
                ....*....|....*....|...
gi 26051218 250 NQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14186 234 HQLLRKNPADRLSLSSVLDHPFM 256
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
14-271 1.99e-47

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: 163.79  E-value: 1.99e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGL---KIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWfG 173
Cdd:cd14662  79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGS-PAPRLKICDFGYSKSSVLHSQPK-S 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVL-RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ----HKLYQQIKAGAYDFpsPEWDTVTPEAKNL 248
Cdd:cd14662 157 TVGTPAYIAPEVLsRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKI--PDYVRVSQDCRHL 234
                       250       260
                ....*....|....*....|...
gi 26051218 249 INQMLTINPAKRITAHEALKHPW 271
Cdd:cd14662 235 LSRIFVANPAKRITIPEIKNHPW 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
13-261 2.60e-47

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 165.76  E-value: 2.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKK-LSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   92 LVTGGELFEDI---------VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAI 162
Cdd:PTZ00263  99 FVVGGELFTHLrkagrfpndVAKFYHAE---------LVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  163 EVQgdqQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpeWdtVT 242
Cdd:PTZ00263 167 KVP---DRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FD 239
                        250
                 ....*....|....*....
gi 26051218  243 PEAKNLINQMLTINPAKRI 261
Cdd:PTZ00263 240 GRARDLVKGLLQTDHTKRL 258
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
18-272 5.38e-47

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: 162.68  E-value: 5.38e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLsardhqkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD-LVTGG 96
Cdd:cd14109  10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF-------LMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDnLASTI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgaAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd14109  83 ELVRDNLlpGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD----KLKLADFGQSRRLLRGKLTTLIY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 aGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLT 254
Cdd:cd14109 159 -GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLV 237
                       250
                ....*....|....*...
gi 26051218 255 INPAKRITAHEALKHPWV 272
Cdd:cd14109 238 YIPESRLTVDEALNHPWF 255
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
20-272 1.27e-46

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: 161.66  E-value: 1.27e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS--ARDHQKLEREARICRLLKHSNIVRLHDSIS--EEGFHYLVFDLVTG 95
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRriPNGEANVKREIQILRRLNHRNVIKLVDVLYneEKQKLYMVMEYCVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFE-DIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQ--GDQQAWF 172
Cdd:cd14119  81 GLQEMlDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTT---DGTLKISDFGVAEALDlfAEDDTCT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAY--GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLIN 250
Cdd:cd14119 158 TSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIP----DDVDPDLQDLLR 233
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWV 272
Cdd:cd14119 234 GMLEKDPEKRFTIEQIRQHPWF 255
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
20-271 1.55e-46

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: 163.17  E-value: 1.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREaricrLLKHSN---IVRLHDSISEEGFHYLVFDLV 93
Cdd:cd05599   9 IGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEqvaHVRAERD-----ILAEADnpwVVKLYYSFQDEENLYLIMEFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAwFG 173
Cdd:cd05599  84 PGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR---GHIKLSDFGLCTGLKKSHLA-YS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQML 253
Cdd:cd05599 160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIERLL 239
                       250       260
                ....*....|....*....|.
gi 26051218 254 TiNPAKRITAH---EALKHPW 271
Cdd:cd05599 240 C-DAEHRLGANgveEIKSHPF 259
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-272 2.91e-46

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: 161.24  E-value: 2.91e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHS-NIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNpRVVNLHEVYETTSEIILILEYAAGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVqGDQQAWFGF 174
Cdd:cd14198  94 EIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKI-GHACELREI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLT 254
Cdd:cd14198 173 MGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFIQKLLV 252
                       250
                ....*....|....*...
gi 26051218 255 INPAKRITAHEALKHPWV 272
Cdd:cd14198 253 KNPEKRPTAEICLSHSWL 270
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
14-285 3.45e-46

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: 161.18  E-value: 3.45e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVK---GADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd14104  79 SGVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTR-RGSYIKIIEFGQSRQLKPGDKFRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAgTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQM 252
Cdd:cd14104 158 QYT-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRL 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 26051218 253 LTINPAKRITAHEALKHPWVCQRS------TVASMMHRQ 285
Cdd:cd14104 237 LVKERKSRMTAQEALNHPWLKQGMetvsskDIKTTRHRR 275
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
14-271 5.59e-46

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: 159.95  E-value: 5.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSI-SEEGFHYLVFD 91
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKfLPRELEILARLNHKSIIKTYEIFeTSDGKVYIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd14165  83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD---KDFNIKLTDFGFSKRCLRDENGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 F----GFAGTPGYLSPEVLRKEAYGKPV-DIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVtpEAK 246
Cdd:cd14165 160 IvlskTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTS--ECK 237
                       250       260
                ....*....|....*....|....*
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14165 238 DLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
12-272 8.61e-46

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: 159.35  E-value: 8.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL--SARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd14116   5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLekAGVEHQ-LRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd14116  84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADFGWSVHAPSSRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLI 249
Cdd:cd14116 161 T--TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFP----DFVTEGARDLI 234
                       250       260
                ....*....|....*....|...
gi 26051218 250 NQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14116 235 SRLLKHNPSQRPMLREVLEHPWI 257
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
11-271 1.16e-45

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: 158.91  E-value: 1.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINT---KKLSARdhqkleREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd14108   1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVrakKKTSAR------RELALLAELDHKSIVRFHDAFEKRRVVI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEVQGD 167
Cdd:cd14108  75 IVTELCHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQ-KTDQVRICDFGNAQELTPN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFaGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd14108 153 EPQYCKY-GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKG 231
                       250       260
                ....*....|....*....|....
gi 26051218 248 LINQMLtINPAKRITAHEALKHPW 271
Cdd:cd14108 232 FIIKVL-VSDRLRPDAEETLEHPW 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
20-272 2.04e-45

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: 158.52  E-value: 2.04e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:cd06623   9 LGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQ-LLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAR-EYYSEADASHCIQQILEAVLHCHQM-GVVHRDLKPENLLLASKckgAAVKLADFGLA--IEvQGDQQAwFGFA 175
Cdd:cd06623  87 ADLLKKvGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSK---GEVKIADFGISkvLE-NTLDQC-NTFV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAyDFPSPEW--DTVTPEAKNLINQML 253
Cdd:cd06623 162 GTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAIC-DGPPPSLpaEEFSPEFRDFISACL 240
                       250
                ....*....|....*....
gi 26051218 254 TINPAKRITAHEALKHPWV 272
Cdd:cd06623 241 QKDPKKRPSAAELLQHPFI 259
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
20-263 4.23e-45

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: 159.40  E-value: 4.23e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK---LEREARIcRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKhimAERNVLL-KNVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd05575  82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQ---GHVVLTDFGLCKEGIEPSDTTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQMLTIN 256
Cdd:cd05575 159 TPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLR----TNVSPSARDLLEGLLQKD 234

                ....*..
gi 26051218 257 PAKRITA 263
Cdd:cd05575 235 RTKRLGS 241
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
13-272 8.25e-45

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: 157.80  E-value: 8.25e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-----------------SARDHQK----LER---EARICRLL 68
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgskaAQGEQAKplapLERvyqEIAILKKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  69 KHSNIVRLHDSISE--EGFHYLVFDLVTGGELFEdIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS 146
Cdd:cd14200  81 DHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 147 KckgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLY 223
Cdd:cd14200 160 D---GHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdsGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALH 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 224 QQIKAGAYDFpsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14200 237 NKIKNKPVEF--PEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
14-268 9.85e-45

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: 156.74  E-value: 9.85e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR---DHQKLE--REARICRLL-KHSNIVRLHDSISEEGFHY 87
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKdgnDFQKLPqlREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYY--SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskCKGAAVKLADFGLAIevq 165
Cdd:cd13993  82 IVLEYCPNGDLFEAITENRIYvgKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLS--QDEGTVKLCDFGLAT--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 gdQQAW---FGfAGTPGYLSPEVL------RKEAYGKPVDIWACGVILYILLVGYPPF-------------WDEDQHkLY 223
Cdd:cd13993 157 --TEKIsmdFG-VGSEFYMAPECFdevgrsLKGYPCAAGDIWSLGIILLNLTFGRNPWkiasesdpifydyYLNSPN-LF 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 26051218 224 QQIKAGAYDFpspewdtvtpeaKNLINQMLTINPAKRITAHEALK 268
Cdd:cd13993 233 DVILPMSDDF------------YNLLRQIFTVNPNNRILLPELQL 265
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
14-271 1.79e-44

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: 156.54  E-value: 1.79e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLK-HSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNL-REVKSLRKLNeHPNIVKLKEVFRENDELYFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGgELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQgDQQA 170
Cdd:cd07830  80 MEG-NLYQLMKDRKgkPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGP---EVVKIADFGLAREIR-SRPP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVI---LYIL------------------LVGYP--PFWDEDQhKLYQQI 226
Cdd:cd07830 155 YTDYVSTRWYRAPEIlLRSTSYSSPVDIWALGCImaeLYTLrplfpgsseidqlykicsVLGTPtkQDWPEGY-KLASKL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 227 kagAYDFPS----------PewdTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07830 234 ---GFRFPQfaptslhqliP---NASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
14-270 2.99e-44

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: 155.06  E-value: 2.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKM---RLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELfEDIVA--REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd06614  79 DGGSL-TDIITqnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKD---GSVKLADFGFAAQLTKEKSKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYDFPSPEwdTVTPEAKNLIN 250
Cdd:cd06614 155 NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRaLFLITTKGIPPLKNPE--KWSPEFKDFLN 232
                       250       260
                ....*....|....*....|
gi 26051218 251 QMLTINPAKRITAHEALKHP 270
Cdd:cd06614 233 KCLVKDPEKRPSAEELLQHP 252
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
20-272 4.56e-44

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: 154.98  E-value: 4.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH--QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14070  10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYvtKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA--IEVQGDQQAWFGFA 175
Cdd:cd14070  90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGLSncAGILGYSDPFSTQC 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDE--DQHKLYQQIKAGAYdfpSPEWDTVTPEAKNLINQML 253
Cdd:cd14070 167 GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEM---NPLPTDLSPGAISFLRSLL 243
                       250
                ....*....|....*....
gi 26051218 254 TINPAKRITAHEALKHPWV 272
Cdd:cd14070 244 EPDPLKRPNIKQALANRWL 262
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
20-271 4.01e-43

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: 154.10  E-value: 4.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHE---YA------AKIINTKKLSArdHQKLEREarICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05584   4 LGKGGYGKVFQVRKTTGSDKgkiFAmkvlkkASIVRNQKDTA--HTKAERN--ILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAaVKLADFGLAIEVQGDQQA 170
Cdd:cd05584  80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL--DAQGH-VKLTDFGLCKESIHDGTV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLIN 250
Cdd:cd05584 157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP----YLTNEARDLLK 232
                       250       260
                ....*....|....*....|....*.
gi 26051218 251 QMLTINPAKRITA----HEALK-HPW 271
Cdd:cd05584 233 KLLKRNVSSRLGSgpgdAEEIKaHPF 258
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
9-267 4.08e-43

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: 152.83  E-value: 4.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKkLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd13996   3 RYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLT-EKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAR---EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGaaVKLADFGLAIEV- 164
Cdd:cd13996  82 QMELCEGGTLRDWIDRRnssSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIGDFGLATSIg 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWF-------------GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWdEDQHKLyQQIKAGAY 231
Cdd:cd13996 160 NQKRELNNlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAM-ERSTIL-TDLRNGIL 237
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 232 dfpsPEW-DTVTPEAKNLINQMLTINPAKRITAHEAL 267
Cdd:cd13996 238 ----PESfKAKHPKEADLIQSLLSKNPEERPSAEQLL 270
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-272 9.04e-43

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: 152.43  E-value: 9.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-------------SARDH-----------QKLEREARICRL 67
Cdd:cd14199   2 NQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprGARAApegctqprgpiERVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  68 LKHSNIVRLHDSISE--EGFHYLVFDLVTGGELFEdIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA 145
Cdd:cd14199  82 LDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 146 skcKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL 222
Cdd:cd14199 161 ---EDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 223 YQQIKAGAYDFpsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14199 238 HSKIKTQPLEF--PDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
20-271 1.71e-42

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: 150.71  E-value: 1.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHS-NIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd05611   4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTnVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfGFAGT 177
Cdd:cd05611  84 CASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDFGLSRNGLEKRHNK-KFVGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINP 257
Cdd:cd05611 160 PDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDP 239
                       250
                ....*....|....*..
gi 26051218 258 AKRITAH---EALKHPW 271
Cdd:cd05611 240 AKRLGANgyqEIKSHPF 256
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
14-272 2.49e-42

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: 150.23  E-value: 2.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSA------RDHQKLEREARICRLLK---HSNIVRLHDSISEEG 84
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVdtwvrdRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGG-ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE 163
Cdd:cd14004  82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN---GTIKLIDFGSAAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQqaWFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDqhklyqQIKAGAYDFPSpewdTVT 242
Cdd:cd14004 159 IKSGP--FDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIE------EILEADLRIPY----AVS 226
                       250       260       270
                ....*....|....*....|....*....|
gi 26051218 243 PEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14004 227 EDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
20-271 6.69e-42

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: 148.96  E-value: 6.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIInTKKLSARdhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFV-SKKMKKK--EQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFgFAGTPG 179
Cdd:cd14115  78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHH-LLGNPE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 180 YLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAK 259
Cdd:cd14115 157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRR 236
                       250
                ....*....|..
gi 26051218 260 RITAHEALKHPW 271
Cdd:cd14115 237 RPTAATCLQHPW 248
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
20-271 7.95e-42

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: 150.58  E-value: 7.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEReaRICRLLKHSNIVRLHDSISEEgfHYLVF--DLVT 94
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDevaHTLTEN--RVLQNTRHPFLTSLKYSFQTN--DRLCFvmEYVN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd05571  79 GGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLD---KDGHIKITDFGLCKEEISYGATTKTF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLT 254
Cdd:cd05571 156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS----TLSPEAKSLLAGLLK 231
                       250       260
                ....*....|....*....|..
gi 26051218 255 INPAKRI-----TAHEALKHPW 271
Cdd:cd05571 232 KDPKKRLgggprDAKEIMEHPF 253
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
14-271 1.14e-41

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: 148.50  E-value: 1.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTK-KLSARDHQklEREarICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRsSTRARAFQ--ERD--ILARLSHRRLTCLLDQFETRKTLILILEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd14107  80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTR-EDIKICDFGFAQEITPSEHQFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFaGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQM 252
Cdd:cd14107 159 KY-GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRV 237
                       250
                ....*....|....*....
gi 26051218 253 LTINPAKRITAHEALKHPW 271
Cdd:cd14107 238 LQPDPEKRPSASECLSHEW 256
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
14-272 1.23e-41

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: 148.15  E-value: 1.23e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIN----TKKLSARDHQKLEREarICRLLK-----HSNIVRLHDSISEEG 84
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrvTEWAMINGPVPVPLE--IALLLKaskpgVPGVIRLLDWYERPD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGGE-LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAIE 163
Cdd:cd14005  80 GFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI--NLRTGEVKLIDFGCGAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQgdQQAWFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEdqhklyQQIKAGAYDFpspeWDTVT 242
Cdd:cd14005 158 LK--DSVYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLF----RPRLS 225
                       250       260       270
                ....*....|....*....|....*....|
gi 26051218 243 PEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14005 226 KECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
12-271 2.74e-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: 148.32  E-value: 2.74e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSArdHQKLER---EARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVK--LKQVEHtlnEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGdq 168
Cdd:cd14209  79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GYIKVTDFGFAKRVKG-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFwDEDQH-KLYQQIKAGAYDFPSpewdTVTPEAKN 247
Cdd:cd14209 154 RTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF-FADQPiQIYEKIVSGKVRFPS----HFSSDLKD 227
                       250       260
                ....*....|....*....|....*....
gi 26051218 248 LINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd14209 228 LLRNLLQVDLTKRFgnlknGVNDIKNHKW 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
20-267 3.99e-41

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: 147.39  E-value: 3.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIInTKKLSARDHQ--KLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14187  15 LGKGGFAKCYEITDADTKEVFAGKIV-PKSLLLKPHQkeKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAGT 177
Cdd:cd14187  94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDME---VKIGDFGLATKVEYDGERKKTLCGT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINP 257
Cdd:cd14187 171 PNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDP 246
                       250
                ....*....|
gi 26051218 258 AKRITAHEAL 267
Cdd:cd14187 247 TARPTINELL 256
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
14-271 4.59e-41

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: 148.83  E-value: 4.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIN--TKKLSarDHQKLEREARICRLLKHSNIVRLHDSI---SEEGFH-- 86
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISnvFDDLI--DAKRILREIKILRHLKHENIIGLLDILrppSPEEFNdv 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVtGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA--IEV 164
Cdd:cd07834  80 YIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCD---LKICDFGLArgVDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPF---WDEDQHKLYQQI-------------- 226
Cdd:cd07834 156 DEDKGFLTEYVVTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFpgrDYIDQLNLIVEVlgtpseedlkfiss 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 227 -KAGAY-----DFPSPEWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07834 236 eKARNYlkslpKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPY 290
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
12-271 6.47e-40

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: 144.77  E-value: 6.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKLSARD-----HQKLEREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd07833   1 NKYEVLGVVGEGAYGVVLKCRNKATG-----EIVAIKKFKESEddedvKKTALREVKVLRQLRHENIVNLKEAFRRKGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVtGGELFEDIVAREYYSEADASH-CIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQ 165
Cdd:cd07833  76 YLVFEYV-ERTLLELLEASPGGLPPDAVRsYIWQLLQAIAYCHSHNIIHRDIKPENILVS---ESGVLKLCDFGFARALT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GD-QQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF---WDEDQHKLYQQ-----IKAGAYDFPS 235
Cdd:cd07833 152 ARpASPLTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFpgdSDIDQLYLIQKclgplPPSHQELFSS 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 236 ---------PEWDT-----------VTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07833 232 nprfagvafPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
20-271 7.72e-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: 144.07  E-value: 7.72e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRrCVKLCTGHE----YAAKIIN-----TKKLSArDHQKLER---EA-RICRLLkhsniVRLHDSISEEGFH 86
Cdd:cd05583   2 LGTGAYGKVF-LVRKVGGHDagklYAMKVLKkativQKAKTA-EHTMTERqvlEAvRQSPFL-----VTLHYAFQTDAKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE-VQ 165
Cdd:cd05583  75 HLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSE---GHVVLTDFGLSKEfLP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAWFGFAGTPGYLSPEVLR--KEAYGKPVDIWACGVILYILLVGYPPFWDED----QHKLYQQIKAGAYDFPSpewd 239
Cdd:cd05583 152 GENDRAYSFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTVDGernsQSEISKRILKSHPPIPK---- 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 240 TVTPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05583 228 TFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPF 264
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
20-226 7.94e-40

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: 145.50  E-value: 7.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK---LEREArICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhimAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVkLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL--DCQGHVV-LTDFGLCKEGMEPEETTSTFCG 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI 226
Cdd:cd05603 159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNI 208
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
20-270 8.35e-40

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: 143.28  E-value: 8.35e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRC-VKLCTGHEYAAKIINTKKLSaRDHQKLEREARICRLLKHSNIVRLHDsISEEGFH-YLVFDLVTGGE 97
Cdd:cd14120   1 IGHGAFAVVFKGrHRKKPDLPVAIKCITKKNLS-KSQNLLGKEIKILKELSHENVVALLD-CQETSSSvYLVMEYCNGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL--ASKCKGAA----VKLADFGLAIEVQGDQQAw 171
Cdd:cd14120  79 LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshNSGRKPSPndirLKIADFGFARFLQDGMMA- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL---YQQIKAGAYDFPSpewdTVTPEAKNL 248
Cdd:cd14120 158 ATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPS----GTSPALKDL 233
                       250       260
                ....*....|....*....|..
gi 26051218 249 INQMLTINPAKRITAHEALKHP 270
Cdd:cd14120 234 LLGLLKRNPKDRIDFEDFFSHP 255
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-272 1.52e-39

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: 143.19  E-value: 1.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtKKLSARDhqKLEREARICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd14113   5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRD--QVTHELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd14113  82 LEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTYY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AwFGFAGTPGYLSPEVLrkeaYGKPV----DIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEA 245
Cdd:cd14113 162 I-HQLLGSPEFAAPEII----LGNPVsltsDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKA 236
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14113 237 KDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
14-272 1.85e-39

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: 142.65  E-value: 1.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFG-------LAIEVQG 166
Cdd:cd14111  82 SGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL---NAIKIVDFGsaqsfnpLSLRQLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQqawfgfAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPSPEWDTVTPEAK 246
Cdd:cd14111 159 RR------TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSAS 231
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14111 232 LFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
20-270 2.33e-39

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: 143.05  E-value: 2.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPfIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGdQQAWFGFAG 176
Cdd:cd05577  81 KYHIynVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDH---GHVRISDLGLAVEFKG-GKKIKGRVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVGYPPFWDE----DQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQ 251
Cdd:cd05577 157 THGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYP----DSFSPEARSLCEG 232
                       250       260
                ....*....|....*....|....
gi 26051218 252 MLTINPAKRI-----TAHEALKHP 270
Cdd:cd05577 233 LLQKDPERRLgcrggSADEVKEHP 256
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
13-271 2.39e-39

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: 144.29  E-value: 2.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFS---VVRRCVKLCTGHEYAAKIIN----TKKLSARDHQKLEREarICRLLKHSN-IVRLHDSISEEG 84
Cdd:cd05614   1 NFELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRkaalVQKAKTVEHTRTERN--VLEHVRQSPfLVTLHYAFQTDA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE- 163
Cdd:cd05614  79 KLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSE---GHVVLTDFGLSKEf 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAWFGFAGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPFWDE----DQHKLYQQIKAGAYDFPSpew 238
Cdd:cd05614 156 LTEEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTLEgeknTQSEVSRRILKCDPPFPS--- 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26051218 239 dTVTPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05614 233 -FIGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPF 269
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
20-226 5.77e-39

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: 143.18  E-value: 5.77e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK---LEREArICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKhimAERNV-LLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd05604  83 ELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQ---GHIVLTDFGLCKEGISNSDTTTTFCG 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI 226
Cdd:cd05604 160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI 209
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
26-271 9.32e-39

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: 140.26  E-value: 9.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  26 SVVRRCVKLCTGHEYAAKIINTKKLsardHQKLEREARicrLLKHSNIVRLHDSISEEGFHYLVFDLvTGGELFEDIVAR 105
Cdd:cd13976   7 SSLYRCVDIHTGEELVCKVVPVPEC----HAVLRAYFR---LPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 106 EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEV 185
Cdd:cd13976  79 KRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER-TKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 186 LRKEAY--GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQMLTINPAKRITA 263
Cdd:cd13976 158 LNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIP----ETLSPRARCLIRSLLRREPSERLTA 233

                ....*...
gi 26051218 264 HEALKHPW 271
Cdd:cd13976 234 EDILLHPW 241
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
20-271 9.70e-39

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: 142.71  E-value: 9.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKevaHTIGERNILVRTALDESPfIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFA 175
Cdd:cd05586  81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDAN---GHIALCDFGLSKADLTDNKTTNTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewDTVTPEAKNLINQMLT 254
Cdd:cd05586 158 GTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPK---DVLSDEGRSFVKGLLN 234
                       250       260
                ....*....|....*....|.
gi 26051218 255 INPAKRITAH----EALKHPW 271
Cdd:cd05586 235 RNPKHRLGAHddavELKEHPF 255
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
13-272 9.85e-39

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: 140.83  E-value: 9.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDS--ISEEgfHYLVF 90
Cdd:cd06647   8 KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSylVGDE--LWVVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd06647  84 EYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYDFPSPEwdTVTPEAKNLI 249
Cdd:cd06647 160 RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSAIFRDFL 237
                       250       260
                ....*....|....*....|...
gi 26051218 250 NQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06647 238 NRCLEMDVEKRGSAKELLQHPFL 260
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
14-272 1.03e-38

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: 140.87  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKlerEARICRLL-KHS-----NIVRLHDSiseegFHY 87
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD---EIRLLELLnKKDkadkyHIVRLKDV-----FYF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 -----LVFDLVtGGELFEDIvarEYYSEADASHC-----IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLAD 157
Cdd:cd14133  73 knhlcIVFELL-SQNLYEFL---KQNKFQYLSLPrirkiAQQILEALVFLHSLGLIHCDLKPENILLASYSR-CQIKIID 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLAIEVqgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFP--- 234
Cdd:cd14133 148 FGSSCFL---TQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPahm 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26051218 235 ---SPEWDtvtPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14133 225 ldqGKADD---ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
20-269 1.74e-38

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: 142.07  E-value: 1.74e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEvAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGFAGTP 178
Cdd:cd05595  83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD---KDGHIKITDFGLCKEGITDGATMKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 179 GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINPA 258
Cdd:cd05595 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPR----TLSPEAKSLLAGLLKKDPK 235
                       250
                ....*....|....*.
gi 26051218 259 KRI-----TAHEALKH 269
Cdd:cd05595 236 QRLgggpsDAKEVMEH 251
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
20-272 1.86e-38

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: 139.85  E-value: 1.86e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAK---IINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 EL---------FEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGD 167
Cdd:cd06632  88 SIhkllqrygaFEEPVIRLY---------TRQILSGLAYLHSRNTVHRDIKGANILVD---TNGVVKLADFGMAKHVEAF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAwFGFAGTPGYLSPEVLRKE--AYGKPVDIWACGVILYILLVGYPPFWDedqhklYQQIKAGAYDFPSPEW----DTV 241
Cdd:cd06632 156 SFA-KSFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQ------YEGVAAIFKIGNSGELppipDHL 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06632 229 SPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
20-263 2.03e-38

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: 141.38  E-value: 2.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFS---VVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05582   3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd05582  83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLSKESIDHEKKAYSFCG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI---KAGAYDFpspewdtVTPEAKNLINQML 253
Cdd:cd05582 160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIlkaKLGMPQF-------LSPEAQSLLRALF 232
                       250
                ....*....|
gi 26051218 254 TINPAKRITA 263
Cdd:cd05582 233 KRNPANRLGA 242
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
20-269 2.08e-38

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: 139.76  E-value: 2.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSaRDHQ--KLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14188   9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVS-KPHQreKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAGT 177
Cdd:cd14188  88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENME---LKVGDFGLAARLEPLEHRRRTICGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINP 257
Cdd:cd14188 165 PNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPS----SLLAPAKHLIASMLSKNP 240
                       250
                ....*....|..
gi 26051218 258 AKRITAHEALKH 269
Cdd:cd14188 241 EDRPSLDEIIRH 252
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
20-271 2.35e-38

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: 140.78  E-value: 2.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS-ARD--HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd07841   8 LGEGTYAVVYKARDKETGRIVAIKKIKLGERKeAKDgiNFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFMETD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 --ELFED--IVareyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEvqgdqqawF 172
Cdd:cd07841  88 leKVIKDksIV----LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV---LKLADFGLARS--------F 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAG--------TPGYLSPEVL-RKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQ-HKLYQQIK-------AGAYD 232
Cdd:cd07841 153 GSPNrkmthqvvTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPgdsDIDQlGKIFEALGtpteenwPGVTS 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 233 FPSP-EWDTVTP------------EAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07841 233 LPDYvEFKPFPPtplkqifpaasdDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
14-270 7.18e-38

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: 138.29  E-value: 7.18e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIV----AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGdqq 169
Cdd:cd08530  82 PFGDLSKLISkrkkKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILL---SAGDLVKIGDLGISKVLKK--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 awfGFA----GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewdTVTPEA 245
Cdd:cd08530 156 ---NLAktqiGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPP---VYSQDL 229
                       250       260
                ....*....|....*....|....*
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd08530 230 QQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
20-271 9.26e-38

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: 139.63  E-value: 9.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR---DHQKLERE--ARIcrllKHSNIVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRsevTHTLAERTvlAQV----DCPFIVPLKFSFQSPEKLYLVLAFIN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd05585  78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYT---GHIALCDFGLCKLNMKDDDKTNTF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQMLT 254
Cdd:cd05585 155 CGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGLLN 230
                       250       260
                ....*....|....*....|
gi 26051218 255 INPAKRI---TAHEALKHPW 271
Cdd:cd05585 231 RDPTKRLgynGAQEIKNHPF 250
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
20-269 9.60e-38

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: 138.14  E-value: 9.60e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLsARDHQ--KLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14189   9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRV-AKPHQreKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAGT 177
Cdd:cd14189  88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME---LKVGDFGLAARLEPPEQRKKTICGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINP 257
Cdd:cd14189 165 PNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA----SLSLPARHLLAGILKRNP 240
                       250
                ....*....|..
gi 26051218 258 AKRITAHEALKH 269
Cdd:cd14189 241 GDRLTLDQILEH 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
20-260 1.20e-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: 137.28  E-value: 1.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcVKLCtGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd13999   1 IGSGSFGEVYK-GKWR-GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAGTP 178
Cdd:cd13999  79 DLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT---VKIADFGLSRIKNSTTEKMTGVVGTP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 179 GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFwdeDQHKLYQQIKAGAYDFPSPEWDTVTPEA-KNLINQMLTINP 257
Cdd:cd13999 156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF---KELSPIQIAAAVVQKGLRPPIPPDCPPElSKLIKRCWNEDP 232

                ...
gi 26051218 258 AKR 260
Cdd:cd13999 233 EKR 235
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
20-272 1.39e-37

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: 137.82  E-value: 1.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVR-----LHdsiSEEgfHYLVFDLVT 94
Cdd:cd06626   8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRyygveVH---REE--VYIFMEYCQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEdiVAReyYSEADASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd06626  83 EGTLEE--LLR--HGRILDEAVIRvytlQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAVKLKNNTTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WF-----GFAGTPGYLSPEVLRK---EAYGKPVDIWACGVILYILLVGYPPfWDEDQHKLYQQIKAGAYDFPS-PEWDTV 241
Cdd:cd06626 156 MApgevnSLVGTPAYMAPEVITGnkgEGHGRAADIWSLGCVVLEMATGKRP-WSELDNEWAIMYHVGMGHKPPiPDSLQL 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06626 235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
17-272 2.31e-37

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: 137.19  E-value: 2.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDIGKGAFSVVrrcvklCTGHEYAA-KIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDS--ISEEgfHYLVF 90
Cdd:cd06648  12 FVKIGEGSTGIV------CIATDKSTgRQVAVKKMDLRKQQRREllfNEVVIMRDYQHPNIVEMYSSylVGDE--LWVVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd06648  84 EFLEGGAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD---GRVKLSDFGFCAQVSKEVPR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagayDFPSP---EWDTVTPEAKN 247
Cdd:cd06648 160 RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIR----DNEPPklkNLHKVSPRLRS 235
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06648 236 FLDRMLVRDPAQRATAAELLNHPFL 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
17-270 2.98e-37

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: 136.79  E-value: 2.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDI---GKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd08220   2 YEKIrvvGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLADFGLAIEVQGDQQAw 171
Cdd:cd08220  82 PGGTLFEYIQQRkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRT--VVKIGDFGISKILSSKSKA- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWdtvTPEAKNLINQ 251
Cdd:cd08220 159 YTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLILS 235
                       250
                ....*....|....*....
gi 26051218 252 MLTINPAKRITAHEALKHP 270
Cdd:cd08220 236 MLHLDPNKRPTLSEIMAQP 254
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
9-272 3.22e-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: 136.92  E-value: 3.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFT-DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR--DHQkLEREARICRLLKHSNIVRLHDSISEEGF 85
Cdd:cd14117   2 KFTiDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvEHQ-LRREIEIQSHLRHPNILRLYNYFHDRKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ 165
Cdd:cd14117  81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK---GELKIADFGWSVHAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEA 245
Cdd:cd14117 158 SLRRR--TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPP----FLSDGS 231
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14117 232 RDLISKLLRYHPSERLPLKGVMEHPWV 258
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
14-271 3.85e-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: 136.65  E-value: 3.85e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSardhqKLEREARICRLLKHSNIVRLHDSIsEEGFH-YLVFDL 92
Cdd:cd14010   2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRP-----EVLNEVRLTHELKHPNVLKFYEWY-ETSNHlWLVVEY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd14010  76 CTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGN---GTLKLSDFGLARREGEILKELF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFA----------------GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSP 236
Cdd:cd14010 153 GQFsdegnvnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPP 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 237 EWDTV-TPEAKNLINQMLTINPAKRITAHEALKHP-W 271
Cdd:cd14010 233 KVSSKpSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
14-272 4.70e-37

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: 136.27  E-value: 4.70e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSI-SEEGFHYLVFD 91
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRfLPRELQIVERLDHKNIIHVYEMLeSADGKIYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskcKGAAVKLADFGLAIEV-QGDQQA 170
Cdd:cd14163  82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL----QGFTLKLTDFGFAKQLpKGGREL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYdfpsPEWDTVTPEAKNL 248
Cdd:cd14163 158 SQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKmLCQQQKGVSL----PGHLGVSRTCQDL 233
                       250       260
                ....*....|....*....|....
gi 26051218 249 INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14163 234 LKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
18-271 1.05e-36

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: 135.11  E-value: 1.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAA-KIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSGAREVVAvKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEVQGDQQAwFGFAG 176
Cdd:cd14121  81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN-PVLKLADFGFAQHLKPNDEA-HSLRG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGA-YDFPS-PEwdtVTPEAKNLINQMLT 254
Cdd:cd14121 159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTrPE---LSADCRDLLLRLLQ 235
                       250
                ....*....|....*..
gi 26051218 255 INPAKRITAHEALKHPW 271
Cdd:cd14121 236 RDPDRRISFEEFFAHPF 252
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
20-271 1.57e-36

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: 135.23  E-value: 1.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE- 97
Cdd:cd05609   8 ISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQiQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDc 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 --LFEDIV------AREYYSEAdashciqqILeAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA-------- 161
Cdd:cd05609  88 atLLKNIGplpvdmARMYFAET--------VL-ALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSkiglmslt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 -------IEVQ----GDQQAWfgfaGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGA 230
Cdd:cd05609 156 tnlyeghIEKDtrefLDKQVC----GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 26051218 231 YDFPSPEwDTVTPEAKNLINQMLTINPAKRI---TAHEALKHPW 271
Cdd:cd05609 232 IEWPEGD-DALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPF 274
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
12-271 1.66e-36

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: 137.67  E-value: 1.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREaricrLLKHSN---IVRLHDSISEEGF 85
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDqlaHVKAERD-----VLAESDspwVVSLYYSFQDAQY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIE-- 163
Cdd:cd05629  76 LYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID---RGGHIKLSDFGLSTGfh 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 -----------VQGDQ--------------------------QAW--------FGFAGTPGYLSPEVLRKEAYGKPVDIW 198
Cdd:cd05629 153 kqhdsayyqklLQGKSnknridnrnsvavdsinltmsskdqiATWkknrrlmaYSTVGTPDYIAPEIFLQQGYGQECDWW 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 199 ACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTiNPAKRI---TAHEALKHPW 271
Cdd:cd05629 233 SLGAIMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLIT-NAENRLgrgGAHEIKSHPF 307
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-279 1.93e-36

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: 137.12  E-value: 1.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARicRLLKHSN---IVRLHDSISEEGFHYL 88
Cdd:cd05596  26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEER--DIMAHANsewIVQLHYAFQDDKYLYM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQ 168
Cdd:cd05596 104 VMDYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD---ASGHLKLADFGTCMKMDKDG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFA-GTPGYLSPEVLRKEA----YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI--KAGAYDFPSPewDTV 241
Cdd:cd05596 180 LVRSDTAvGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKImnHKNSLQFPDD--VEI 257
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 242 TPEAKNLINQMLTI-------NPAKRITAHEALKH---PWVCQRSTVA 279
Cdd:cd05596 258 SKDAKSLICAFLTDrevrlgrNGIEEIKAHPFFKNdqwTWDNIRETVP 305
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
13-272 3.20e-36

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: 134.37  E-value: 3.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCV-KLCTGHEYAAKIINTKKLsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRhKEKHDLEVAVKCINKKNL-AKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA------SKCKGAAVKLADFGLAIEVQ 165
Cdd:cd14202  82 YCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIRIKIADFGFARYLQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPeA 245
Cdd:cd14202 162 NNMMA-ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSSH-L 239
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14202 240 RQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
13-268 4.45e-36

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: 133.55  E-value: 4.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS-ARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMdAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGD 167
Cdd:cd08224  81 LADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITAN---GVVKLGDLGLGRFFSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ--HKLYQQIKAGAYDfPSPEwDTVTPEA 245
Cdd:cd08224 158 TTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMnlYSLCKKIEKCEYP-PLPA-DLYSQEL 235
                       250       260
                ....*....|....*....|...
gi 26051218 246 KNLINQMLTINPAKRITAHEALK 268
Cdd:cd08224 236 RDLVAACIQPDPEKRPDISYVLD 258
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
1-272 5.03e-36

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: 134.47  E-value: 5.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   1 MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDS- 79
Cdd:cd06655   8 LRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKK--ELIINEILVMKELKNPNIVNFLDSf 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  80 -ISEEGFhyLVFDLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADF 158
Cdd:cd06655  86 lVGDELF--VVMEYLAGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYDFPSPE 237
Cdd:cd06655 160 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE 239
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 238 wdTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06655 240 --KLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFL 272
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
20-270 6.52e-36

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: 134.65  E-value: 6.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVV-----RRCVKLctgheYAAKIIntKKLSARDHQKLE---REARICRL-LKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05570   3 LGKGSFGKVmlaerKKTDEL-----YAIKVL--KKEVIIEDDDVEctmTEKRVLALaNRHPFLTGLHACFQTEDRLYFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05570  76 EYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAE---GHIKIADFGMCKEGIWGGNT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLIN 250
Cdd:cd05570 153 TSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPR----WLSREAVSILK 228
                       250       260
                ....*....|....*....|....*
gi 26051218 251 QMLTINPAKRI-----TAHEALKHP 270
Cdd:cd05570 229 GLLTKDPARRLgcgpkGEADIKAHP 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
14-272 9.70e-36

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: 133.55  E-value: 9.70e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDH---QKLEREARICRLLK---HSNIVRLHD----SISEE 83
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV---RVPLSEEgipLSTIREIALLKQLEsfeHPNVVRLLDvchgPRTDR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFH-YLVF-----DLVTggelFEDIVAREYYSEADASHCIQQILEAV--LHCHQmgVVHRDLKPENLLLASKCKgaaVKL 155
Cdd:cd07838  78 ELKlTLVFehvdqDLAT----YLDKCPKPGLPPETIKDLMRQLLRGLdfLHSHR--IVHRDLKPQNILVTSDGQ---VKL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 156 ADFGLAiEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVI---LYILLVGYPPFWDEDQ-HKLYQQI-KAGA 230
Cdd:cd07838 149 ADFGLA-RIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIfaeLFNRRPLFRGSSEADQlGKIFDVIgLPSE 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 231 YDFP---SPEWDT---------------VTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07838 228 EEWPrnsALPRSSfpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
14-271 1.08e-35

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: 133.17  E-value: 1.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLK-HSNIVRLHDSISEE--GFHYLVF 90
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNL-REIQALRRLSpHPNILRLIEVLFDRktGRLALVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGgELFEDIVAREYY-SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaaVKLADFGLAIEVQgDQQ 169
Cdd:cd07831  80 ELMDM-NLYELIKGRKRPlPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI----LKLADFGSCRGIY-SKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFWDEDQ-------H--------KLYQQIKAGA--- 230
Cdd:cd07831 154 PYTEYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiakiHdvlgtpdaEVLKKFRKSRhmn 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 231 YDFPSPEwDT--------VTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07831 234 YNFPSKK-GTglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
13-272 1.45e-35

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: 132.44  E-value: 1.45e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCV-KLCTGHEYAAKIINTKKLSaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14201   7 EYSRKDLVGHGAFAVVFKGRhRKKTDWEVAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA------SKCKGAAVKLADFGLAIEVQ 165
Cdd:cd14201  86 YCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkSSVSGIRIKIADFGFARYLQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYDFPSpewdTVT 242
Cdd:cd14201 166 SNMMA-ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQansPQDLRMFYEKNKNLQPSIPR----ETS 240
                       250       260       270
                ....*....|....*....|....*....|
gi 26051218 243 PEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14201 241 PYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
2-271 1.45e-35

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: 134.44  E-value: 1.45e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   2 ATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSI 80
Cdd:cd05593   5 STTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEvAHTLTESRVLKNTRHPFLTSLKYSF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGL 160
Cdd:cd05593  85 QTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD---KDGHIKITDFGL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdT 240
Cdd:cd05593 162 CKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----T 237
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 26051218 241 VTPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05593 238 LSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 273
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
12-269 1.47e-35

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: 134.77  E-value: 1.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05594  25 NDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEvAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd05594 105 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLD---KDGHIKITDFGLCKEGIKDGA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLI 249
Cdd:cd05594 182 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLSPEAKSLL 257
                       250       260
                ....*....|....*....|....*
gi 26051218 250 NQMLTINPAKRI-----TAHEALKH 269
Cdd:cd05594 258 SGLLKKDPKQRLgggpdDAKEIMQH 282
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
12-270 1.47e-35

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: 132.48  E-value: 1.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSArDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQT-SMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFeDIVAREY----YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLA--IEVQ 165
Cdd:cd06610  80 LLSGGSLL-DIMKSSYprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL---GEDGSVKIADFGVSasLATG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQ--AWFGFAGTPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGayDFPSPEWDT-- 240
Cdd:cd06610 156 GDRTrkVRKTFVGTPCWMAPEVMEQVrGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQN--DPPSLETGAdy 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 241 --VTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd06610 234 kkYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
14-272 2.06e-35

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: 131.78  E-value: 2.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntKKLSARDHQKLE-----REARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVL--KEISVGELQPDEtvdanREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVA-REYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLaskcKGAAVKLADFGLAIEV 164
Cdd:cd08222  80 VTEYCEGGDLDDKISEyKKSGTTIDENQILDwfiQLLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISRIL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGayDFPS-PewDTVTP 243
Cdd:cd08222 156 MGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEG--ETPSlP--DKYSK 231
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd08222 232 ELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
12-271 2.18e-35

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: 133.63  E-value: 2.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRrCVKL-CTGHEYAAKIINTKKLSARDHQKLEREARicRLLKHSN---IVRLHDSISEEGFHY 87
Cdd:cd05597   1 DDFEILKVIGRGAFGEVA-VVKLkSTEKVYAMKILNKWEMLKRAETACFREER--DVLVNGDrrwITKLHYAFQDENYLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGEL------FEDI----VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLAD 157
Cdd:cd05597  78 LVMDYYCGGDLltllskFEDRlpeeMARFYLAE---------MVLAIDSIHQLGYVHRDIKPDNVLLD---RNGHIRLAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLAIEVQGDQQAWFGFA-GTPGYLSPEVLR-----KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI--KAG 229
Cdd:cd05597 146 FGSCLKLREDGTVQSSVAvGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKE 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 26051218 230 AYDFPSPEwDTVTPEAKNLINQMLTInPAKRI---TAHEALKHPW 271
Cdd:cd05597 226 HFSFPDDE-DDVSEEAKDLIRRLICS-RERRLgqnGIDDFKKHPF 268
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
13-270 2.84e-35

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: 131.38  E-value: 2.84e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAiEVQGDQQa 170
Cdd:cd08529  81 AENGDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD---KGDNVKIGDLGVA-KILSDTT- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 wfGFA----GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPSPEwdTVTPEAK 246
Cdd:cd08529 156 --NFAqtivGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYP-PISA--SYSQDLS 230
                       250       260
                ....*....|....*....|....
gi 26051218 247 NLINQMLTINPAKRITAHEALKHP 270
Cdd:cd08529 231 QLIDSCLTKDYRQRPDTTELLRNP 254
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
13-272 2.92e-35

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: 131.47  E-value: 2.92e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd08218   1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd08218  81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGIARVLNSTVEL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWdtvTPEAKNLIN 250
Cdd:cd08218 158 ARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRY---SYDLRSLVS 234
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWV 272
Cdd:cd08218 235 QLFKRNPRDRPSINSILEKPFI 256
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
13-270 4.07e-35

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: 130.58  E-value: 4.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLK-HSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA--IEVQG 166
Cdd:cd13997  81 LCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK---GTCKIGDFGLAtrLETSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQawfgfAGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYP-PfwdeDQHKLYQQIKAGayDFPSPEWDTVTPE 244
Cdd:cd13997 158 DVE-----EGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPlP----RNGQQWQQLRQG--KLPLPPGLVLSQE 226
                       250       260
                ....*....|....*....|....*.
gi 26051218 245 AKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd13997 227 LTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
20-272 4.57e-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: 130.94  E-value: 4.57e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSA---RDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd06625   8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTeasKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQG--DQQAWFGF 174
Cdd:cd06625  88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSN---GNVKLGDFGASKRLQTicSSTGMKSV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYqQIkagAYDFPSPEW-DTVTPEAKNLINQM 252
Cdd:cd06625 165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIF-KI---ATQPTNPQLpPHVSEDARDFLSLI 240
                       250       260
                ....*....|....*....|
gi 26051218 253 LTINPAKRITAHEALKHPWV 272
Cdd:cd06625 241 FVRNKKQRPSAEELLSHSFV 260
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
14-271 4.63e-35

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: 131.53  E-value: 4.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTkklsarDHQKLE------REARICRLLKHSNIVRLHDSISEEGFH- 86
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRM------ENEKEGfpitaiREIKLLQKLDHPNVVRLKEIVTSKGSAk 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 -----YLVF-----DLvTGgelfediVAREYYSEADASH--CI-QQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAV 153
Cdd:cd07840  75 ykgsiYMVFeymdhDL-TG-------LLDNPEVKFTESQikCYmKQLLEGLQYLHSNGILHRDIKGSNILINND---GVL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 154 KLADFGLAIEVQGDQQAWFgfagTPG-----YLSPEVLRKE-AYGKPVDIWACGVILYILLVGYPPF------------- 214
Cdd:cd07840 144 KLADFGLARPYTKENNADY----TNRvitlwYRPPELLLGAtRYGPEVDMWSVGCILAELFTGKPIFqgkteleqlekif 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 215 ----------WDE-DQHKLYQQIKAgAYDFPSPEWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07840 220 elcgspteenWPGvSDLPWFENLKP-KKPYKRRLREVFknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
14-281 7.72e-35

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: 130.67  E-value: 7.72e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSaRDHQKLEREARICRLLKHS---NIVRLHDSISEEGFHYLVF 90
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD-DDVSDIQKEVALLSQLKLGqpkNIIKYYGSYLKGPSLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQA 170
Cdd:cd06917  82 DYCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLCDFGVAASLNQNSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYdfPSPEWDTVTPEAKNLI 249
Cdd:cd06917 158 RSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKP--PRLEGNGYSPLLKEFV 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 250 NQMLTINPAKRITAHEALKHPWVCQRSTVASM 281
Cdd:cd06917 236 AACLDEEPKDRLSADELLKSKWIKQHSKTPTS 267
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-271 1.12e-34

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: 130.89  E-value: 1.12e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFS---VVRRCVKLCTGHEYAAKIIN----TKKLSARDHQKLEREaricrLLKHSN----IVRLHDSISE 82
Cdd:cd05613   2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKkatiVQKAKTAEHTRTERQ-----VLEHIRqspfLVTLHYAFQT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAI 162
Cdd:cd05613  77 DTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSS---GHVVLTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQ-QAWFGFAGTPGYLSPEVLR--KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWD 239
Cdd:cd05613 154 EFLLDEnERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQ 233
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 240 TVTPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05613 234 EMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPF 270
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
14-271 1.81e-34

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: 129.72  E-value: 1.81e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDhqklE-------REARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI---RLETED----EgvpstaiREISLLKELNHPNIVRLLDVVHSENKL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFD-LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAievq 165
Cdd:cd07835  74 YLVFEfLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTE---GALKLADFGLA---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 gdqQAwFGF--------AGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFWDE---DQ-HKLYQ-------Q 225
Cdd:cd07835 147 ---RA-FGVpvrtytheVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDseiDQlFRIFRtlgtpdeD 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 226 IKAGAYDFPS-----PEWDTVT---------PEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07835 223 VWPGVTSLPDykptfPKWARQDlskvvpsldEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
13-263 2.39e-34

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: 130.91  E-value: 2.39e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK--LEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05602   8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKhiMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05602  88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQ---GHIVLTDFGLCKENIEPNGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIkagaYDFPSPEWDTVTPEAKNLIN 250
Cdd:cd05602 165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLE 240
                       250
                ....*....|...
gi 26051218 251 QMLTINPAKRITA 263
Cdd:cd05602 241 GLLQKDRTKRLGA 253
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
13-271 3.69e-34

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: 128.99  E-value: 3.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLK-HSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVtGGELFEdiVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA-IEVQGD 167
Cdd:cd07832  81 YM-LSSLSE--VLRDEerpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISST---GVLKIADFGLArLFSEED 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVL---RKeaYGKPVDIWACGVILYILLVGYPPFWDEDQ---------------HKLYQQIK-- 227
Cdd:cd07832 155 PRLYSHQVATRWYRAPELLygsRK--YDEGVDLWAVGCIFAELLNGSPLFPGENDieqlaivlrtlgtpnEKTWPELTsl 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 26051218 228 --AGAYDFP-SP--EWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07832 233 pdYNKITFPeSKgiRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
12-274 3.73e-34

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: 130.50  E-value: 3.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAakiinTKKLSARDHQKLE----REARICRLLKHSNIVRLHD---SISEEG 84
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVA-----IKKISPFEHQTYClrtlREIKILLRFKHENIIGILDiqrPPTFES 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FH--YLVfdlvtgGELFEDIVAREYYSEaDAS--HC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLAD 157
Cdd:cd07849  80 FKdvYIV------QELMETDLYKLIKTQ-HLSndHIqyfLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCD---LKICD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLA--IEVQGDQQAWFG-FAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH------------- 220
Cdd:cd07849 150 FGLAriADPEHDHTGFLTeYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLhqlnlilgilgtp 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 221 ---KLYQQIKAGAYDF-------PSPEWDTVTPEAKN----LINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd07849 230 sqeDLNCIISLKARNYikslpfkPKVPWNKLFPNADPkaldLLDKMLTFNPHKRITVEEALAHPYLEQ 297
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
20-278 5.45e-34

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: 129.74  E-value: 5.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKL-EREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd05601   9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFfEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 ----------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ 168
Cdd:cd05601  89 lsllsryddiFEESMARFYLAE---------LVLAIHSLHSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFA-GTPGYLSPEVL------RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTV 241
Cdd:cd05601 157 TVTSKMPvGTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKV 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 26051218 242 TPEAKNLINQMLTiNPAKRITAHEALKHP------WVCQRSTV 278
Cdd:cd05601 237 SESAVDLIKGLLT-DAKERLGYEGLCCHPffsgidWNNLRQTV 278
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
28-271 1.13e-33

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: 126.69  E-value: 1.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  28 VRRCVKLCTGHEYAAKIINTKKLSardhqklEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLvTGGELFEDIVAREY 107
Cdd:cd14022   9 VFRAVHLHSGEELVCKVFDIGCYQ-------ESLAPCFCLPAHSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 108 YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLR 187
Cdd:cd14022  81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 188 KEAY--GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPspewDTVTPEAKNLINQMLTINPAKRITAHE 265
Cdd:cd14022 160 TSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQE 235

                ....*.
gi 26051218 266 ALKHPW 271
Cdd:cd14022 236 ILDHPW 241
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
12-290 1.28e-33

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: 128.18  E-value: 1.28e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYED---IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDS--ISEEgfH 86
Cdd:cd06659  18 DPRQLLENyvkIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRR--ELLFNEVVIMRDYQHPNVVEMYKSylVGEE--L 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQG 166
Cdd:cd06659  94 WVLMEYLQGGAL-TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGR---VKLSDFGFCAQISK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagayDFPSPEWDT---VTP 243
Cdd:cd06659 170 DVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLR----DSPPPKLKNshkASP 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMM-----HRQETVEC 290
Cdd:cd06659 246 VLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVpliqqYRKRTSTC 297
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
30-272 1.49e-33

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: 126.15  E-value: 1.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  30 RCVKLCTGHEYAAKIINTKKLsardHQKLEREARicrLLKHSNIVRLHDSISEEGFHYLVFDlVTGGELFEDIVAREYYS 109
Cdd:cd14024  11 RAEHYQTEKEYTCKVLSLRSY----QECLAPYDR---LGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 110 EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS--KCKGAAVKLADfglAIEVQGDQQAWFGFAGTPGYLSPEVL- 186
Cdd:cd14024  83 EDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDelRTKLVLVNLED---SCPLNGDDDSLTDKHGCPAYVGPEILs 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 187 -RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINPAKRITAHE 265
Cdd:cd14024 160 sRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPA----WLSPGARCLVSCMLRRSPAERLKASE 235

                ....*..
gi 26051218 266 ALKHPWV 272
Cdd:cd14024 236 ILLHPWL 242
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-272 3.71e-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: 126.21  E-value: 3.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE-AEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd06609  80 YCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEE---GDVKLADFGVSGQLTSTMSKR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI-KAGAydfPSPEWDTVTPEAKNLIN 250
Cdd:cd06609 156 NTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIpKNNP---PSLEGNKFSKPFKDFVE 232
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWV 272
Cdd:cd06609 233 LCLNKDPKERPSAKELLKHKFI 254
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
14-271 4.29e-33

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: 125.89  E-value: 4.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKI--INT-----KKLSARDHqkLEREARICRLLKHSNIVRLHDS--ISEEG 84
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqLNKdwseeKKQNYIKH--ALREYEIHKSLDHPRIVKLYDVfeIDTDS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FhYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAI 162
Cdd:cd13990  80 F-CTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALkyLNEIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWFG------FAGTPGYLSPEVLrkEAYGKP------VDIWACGVILYILLVGYPPF-WDEDQHKLYQQ---I 226
Cdd:cd13990 159 IMDDESYNSDGmeltsqGAGTYWYLPPECF--VVGKTPpkisskVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEEntiL 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 26051218 227 KAGAYDFPSPewDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd13990 237 KATEVEFPSK--PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
20-271 5.14e-33

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: 127.05  E-value: 5.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREAricrLLKHSN--IVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05598   9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNqvaHVKAERDI----LAEADNewVVKLYYSFQDKENLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIevqgdqqawfGF 174
Cdd:cd05598  85 GGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCT----------GF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 --------------AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW----DEDQHKL-----YQQIKAGAy 231
Cdd:cd05598 152 rwthdskyylahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLaqtpAETQLKVinwrtTLKIPHEA- 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 26051218 232 dfpspewdTVTPEAKNLINQMLTiNPAKRITAHEALK---HPW 271
Cdd:cd05598 231 --------NLSPEAKDLILRLCC-DAEDRLGRNGADEikaHPF 264
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
14-272 6.92e-33

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: 124.97  E-value: 6.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVrrcvKLCTGHEY----AAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSIS-EEGFHY 87
Cdd:cd14164   2 YTLGTTIGEGSFSKV----KLATSQKYcckvAIKIVDRRRASPDFVQKfLPRELSILRRVNHPNIVQMFECIEvANGRLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDlVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkcKGAAVKLADFGLAIEVQGD 167
Cdd:cd14164  78 IVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSA--DDRKIKIADFGFARFVEDY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYdfpsPEWDTVTPEAK 246
Cdd:cd14164 155 PELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLY----PSGVALEEPCR 230
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14164 231 ALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
11-272 7.85e-33

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: 124.65  E-value: 7.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14110   2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKP---EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ-- 168
Cdd:cd14110  79 ELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEK---NLLKIVDLGNAQPFNQGKvl 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 -QAWFGFAGTPgyLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFpSPEWDTVTPEAKN 247
Cdd:cd14110 156 mTDKKGDYVET--MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQL-SRCYAGLSGGAVN 232
                       250       260
                ....*....|....*....|....*
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14110 233 FLKSTLCAKPWGRPTASECLQNPWL 257
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-260 9.90e-33

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: 124.92  E-value: 9.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAF-SVVRRCVKLCTGHEYAAKIINTKKLSARDHQKlER---------EARICR-LLKHSNIVRLHDSIS 81
Cdd:cd08528   1 EYAVLELLGSGAFgCVYKVRKKSNGQTLLALKEINMTNPAFGRTEQ-ERdksvgdiisEVNIIKeQLRHPNIVRYYKTFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 EEGFHYLVFDLVTG---GELFEDIVAR-EYYSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLASKCKgaaVKLA 156
Cdd:cd08528  80 ENDRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK---VTIT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 157 DFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPSP 236
Cdd:cd08528 157 DFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE-PLP 235
                       250       260
                ....*....|....*....|....
gi 26051218 237 EwDTVTPEAKNLINQMLTINPAKR 260
Cdd:cd08528 236 E-GMYSDDITFVIRSCLTPDPEAR 258
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
20-272 1.11e-32

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: 124.47  E-value: 1.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRrCVKLCTGHEYAAKII----NTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd06631   9 LGKGAYGTVY-CGLTSTGQLIAVKQVeldtSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GEL---------FEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA----- 161
Cdd:cd06631  88 GSIasilarfgaLEEPVFCRY---------TKQILEGVAYLHNNNVIHRDIKGNNIMLMPN---GVIKLIDFGCAkrlci 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 -IEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDqhKLYQQIKAGAYDFPSPEW-D 239
Cdd:cd06631 156 nLSSGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMN--PMAAIFAIGSGRKPVPRLpD 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 240 TVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06631 234 KFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
14-274 1.22e-32

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: 126.13  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKL-----SARDHQKLEREARICR-LLKHSNIVRLHDSISEEGFH- 86
Cdd:cd07852   9 YEILKKLGKGAYGIVWKAIDKKTG-----EVVALKKIfdafrNATDAQRTFREIMFLQeLNDHPNIIKLLNVIRAENDKd 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 -YLVFDL-------VTGGELFEDIVAReyyseadasHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADF 158
Cdd:cd07852  84 iYLVFEYmetdlhaVIRANILEDIHKQ---------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCR---VKLADF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLA-----IEVQGDQQAWFGFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPFWDE---DQ-HKLYQQI-K 227
Cdd:cd07852 152 GLArslsqLEEDDENPVLTDYVATRWYRAPEILLGsTRYTKGVDMWSVGCILGEMLLGKPLFPGTstlNQlEKIIEVIgR 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 228 AGAYD---FPSPEWDTV-------------------TPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd07852 232 PSAEDiesIQSPFAATMleslppsrpksldelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
66-271 1.51e-32

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: 123.62  E-value: 1.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  66 RLLKHSNIVRLHDSISEEGFHYLVFDlVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA 145
Cdd:cd14023  40 QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFS 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 146 SKCKgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAY--GKPVDIWACGVILYILLVGYPPFWDEDQHKLY 223
Cdd:cd14023 119 DEER-TQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDSDPSALF 197
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 224 QQIKAGAYDFPspewDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14023 198 SKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
20-271 2.47e-32

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: 123.59  E-value: 2.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkleREARI-CRLLKHSNIVRLHD-SISEEGFHYLVFDLVTGGE 97
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL---REYNIsLELSVHPHIIKTYDvAFETEDYYVFAQEYAPYGD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-CKgaAVKLADFGLAIEVQGDQQAwfgFAG 176
Cdd:cd13987  78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKdCR--RVKLCDFGLTRRVGSTVKR---VSG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLR-KEAYG----KPVDIWACGVILYILLVGYPPfWDEDQHK--------LYQQIKAGAydfPSPEWDTVTP 243
Cdd:cd13987 153 TIPYTAPEVCEaKKNEGfvvdPSIDVWAFGVLLFCCLTGNFP-WEKADSDdqfyeefvRWQKRKNTA---VPSQWRRFTP 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 244 EAKNLINQMLTINPAKRITA---HEALKHPW 271
Cdd:cd13987 229 KALRMFKKLLAPEPERRCSIkevFKYLGDRW 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
13-272 2.54e-32

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: 124.45  E-value: 2.54e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06656  20 KYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd06656  98 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYDFPSPEwdTVTPEAKNLINQ 251
Cdd:cd06656 174 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--RLSAVFRDFLNR 251
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd06656 252 CLEMDVDRRGSAKELLQHPFL 272
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
14-272 2.57e-32

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: 123.53  E-value: 2.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd08225  82 DGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKN--GMVAKLGDFGIARQLNDSMELA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWdtvTPEAKNLINQ 251
Cdd:cd08225 160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLISQ 236
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd08225 237 LFKVSPRDRPSITSILKRPFL 257
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
13-270 3.83e-32

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: 123.09  E-value: 3.83e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRcVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHS-NIVRL--HDSISEEGFHYLV 89
Cdd:cd14131   2 PYEILKQLGKGGSSKVYK-VLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLydYEVTDEDDYLYMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLvtgGEL-FEDIVAREYYSEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKckgaAVKLADFGLAIEVQ 165
Cdd:cd14131  81 MEC---GEIdLATILKKKRPKPIDPNFIRyywKQMLEAVHTIHEEGIVHSDLKPANFLLVKG----RLKLIDFGIAKAIQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GD-------QQawfgfAGTPGYLSPEVLR--------KEAY--GKPVDIWACGVILYILLVGYPPFwdedQH--KLYQQI 226
Cdd:cd14131 154 NDttsivrdSQ-----VGTLNYMSPEAIKdtsasgegKPKSkiGRPSDVWSLGCILYQMVYGKTPF----QHitNPIAKL 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 227 KA---GAYDFPSPEwdtVTPeaKNLINQM---LTINPAKRITAHEALKHP 270
Cdd:cd14131 225 QAiidPNHEIEFPD---IPN--PDLIDVMkrcLQRDPKKRPSIPELLNHP 269
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
20-261 3.97e-32

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: 124.73  E-value: 3.97e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLER-EARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMvEKRVLALSgKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAGT 177
Cdd:cd05616  88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSE---GHIKIADFGMCKENIWDGVTTKTFCGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINP 257
Cdd:cd05616 165 PDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK----SMSKEAVAICKGLMTKHP 240

                ....
gi 26051218 258 AKRI 261
Cdd:cd05616 241 GKRL 244
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
20-271 8.73e-32

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: 123.50  E-value: 8.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhqKLER---EARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05574   9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRN--KVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELF------------EDiVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLA--- 161
Cdd:cd05574  87 ELFrllqkqpgkrlpEE-VARFYAAE---------VLLALEYLHLLGFVYRDLKPENILLH---ESGHIMLTDFDLSkqs 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 -----IEVQGDQQAWFG---------------------FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW 215
Cdd:cd05574 154 svtppPVRKSLRKGSRRssvksieketfvaepsarsnsFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFK 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 216 DEDQHKLYQQIKAGAYDFpsPEWDTVTPEAKNLINQMLTINPAKRI----TAHEALKHPW 271
Cdd:cd05574 234 GSNRDETFSNILKKELTF--PESPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPF 291
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
12-270 1.00e-31

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: 124.22  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD--HQ-KLEREAriCRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNmvHQvQAERDA--LALSKSPFIVHLYYSLQSANNVYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGL-------- 160
Cdd:cd05610  82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE---GHIKLTDFGLskvtlnre 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 --------------------------------------------------AIEVQGDQqawfgFAGTPGYLSPEVLRKEA 190
Cdd:cd05610 159 lnmmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgAARVEGER-----ILGTPDYLAPELLLGKP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 191 YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagAYDFPSPEWD-TVTPEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd05610 234 HGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNIL--NRDIPWPEGEeELSVNAQNAIEILLTMDPTKRAGLKELKQH 311

                .
gi 26051218 270 P 270
Cdd:cd05610 312 P 312
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
13-272 1.16e-31

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: 121.75  E-value: 1.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYED-----IGKGAFSVVrrcvklctgheYAAKIINTKKLSA---------RDHQKLEREARICRLLKHSNIVRLHD 78
Cdd:cd06624   4 EYEYDESgervvLGKGTFGVV-----------YAARDLSTQVRIAikeiperdsREVQPLHEEIALHSRLSHKNIVQYLG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  79 SISEEGFHYLVFDLVTGGEL-----------FEDIVAREYYSeadashciQQILEAVLHCHQMGVVHRDLKPENLLLASk 147
Cdd:cd06624  73 SVSEDGFFKIFMEQVPGGSLsallrskwgplKDNENTIGYYT--------KQILEGLKYLHDNKIVHRDIKGDNVLVNT- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 cKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRK--EAYGKPVDIWACGVILYILLVGYPPFWD--EDQHKLY 223
Cdd:cd06624 144 -YSGVVKISDFGTSKRLAGINPCTETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMF 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 224 qqiKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06624 223 ---KVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
13-272 1.48e-31

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: 121.26  E-value: 1.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI---KLEPGDDfEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELfEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd06613  78 YCGGGSL-QDIYQVtGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLT---EDGDVKLADFGVSAQLTATIAK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPE----WdtvTP 243
Cdd:cd06613 154 RKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKLKdkekW---SP 230
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06613 231 DFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
20-261 1.74e-31

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: 121.91  E-value: 1.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD-HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDI--VAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd05608  89 RYHIynVDEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD---GNVRISDLGLAVELKDGQTKTKGY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLT 254
Cdd:cd05608 166 AGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEALLA 245

                ....*..
gi 26051218 255 INPAKRI 261
Cdd:cd05608 246 KDPEKRL 252
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
9-272 1.83e-31

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: 122.22  E-value: 1.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTkklsarDHQK------LEREARICRLLKHSNIVRLHDSIS- 81
Cdd:cd07864   4 RCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRL------DNEKegfpitAIREIKILRQLNHRSVVNLKEIVTd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 ---------EEGFHYLVF-----DLVtgGELFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK 147
Cdd:cd07864  78 kqdaldfkkDKGAFYLVFeymdhDLM--GLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 CKgaaVKLADFGLA-IEVQGDQQAWFGFAGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPFwDEDQHKLYQQ 225
Cdd:cd07864 153 GQ---IKLADFGLArLYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIF-QANQELAQLE 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 226 IKAGAYDFPSPE----------WDTVTP-----------------EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07864 229 LISRLCGSPCPAvwpdviklpyFNTMKPkkqyrrrlreefsfiptPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
20-261 2.42e-31

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: 122.50  E-value: 2.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIKIL--KKdviIQDDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFVMEYVNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE-VQGDQQAwFGF 174
Cdd:cd05587  82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAE---GHIKIADFGMCKEgIFGGKTT-RTF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLT 254
Cdd:cd05587 158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICKGLLT 233

                ....*..
gi 26051218 255 INPAKRI 261
Cdd:cd05587 234 KHPAKRL 240
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
70-270 2.60e-31

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: 120.84  E-value: 2.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  70 HSNIVRLHDSISEEGFHYLV--------FDLVTGGELFedivAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPEN 141
Cdd:cd13982  54 HPNVIRYFCTEKDRQFLYIAlelcaaslQDLVESPRES----KLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 142 LLLA-SKCKGAA-VKLADFGLAIEVQGDQQAWF---GFAGTPGYLSPEVLRKEAYGKP---VDIWACG-VILYILLVGYP 212
Cdd:cd13982 130 ILIStPNAHGNVrAMISDFGLCKKLDVGRSSFSrrsGVAGTSGWIAPEMLSGSTKRRQtraVDIFSLGcVFYYVLSGGSH 209
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 213 PFWDedqhKLYQQ--IKAGAYDFPSPEWD-TVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd13982 210 PFGD----KLEREanILKGKYSLDKLLSLgEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
13-272 3.24e-31

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: 121.37  E-value: 3.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06654  21 KYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd06654  99 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRS 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYDFPSPEwdTVTPEAKNLINQ 251
Cdd:cd06654 175 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSAIFRDFLNR 252
                       250       260
                ....*....|....*....|.
gi 26051218 252 MLTINPAKRITAHEALKHPWV 272
Cdd:cd06654 253 CLEMDVEKRGSAKELLQHQFL 273
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
17-282 3.25e-31

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: 121.28  E-value: 3.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDIGKGAFSVVrrCVKLCtghEYAAKIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd06657  25 FIKIGEGSTGIV--CIATV---KSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFG 173
Cdd:cd06657 100 EGGAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGR---VKLSDFGFCAQVSKEVPRRKS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagayDFPSPEWDT---VTPEAKNLIN 250
Cdd:cd06657 176 LVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR----DNLPPKLKNlhkVSPSLKGFLD 251
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 251 QMLTINPAKRITAHEALKHPWVCQRSTVASMM 282
Cdd:cd06657 252 RLLVRDPAQRATAAELLKHPFLAKAGPPSCIV 283
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
20-271 3.33e-31

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: 122.48  E-value: 3.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSI---SEEGFH--YLVFDLVT 94
Cdd:cd07858  13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMpppHREAFNdvYIVYELMD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GgELFEDIVAREYYSEadaSHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAW 171
Cdd:cd07858  93 T-DLHQIIRSSQTLSD---DHCqyfLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCD---LKICDFGLARTTSEKGDFM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPFWDED---QHKLYQQI---------------KAGAY- 231
Cdd:cd07858 166 TEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDyvhQLKLITELlgspseedlgfirneKARRYi 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 232 ----DFP----SPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07858 246 rslpYTPrqsfARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPY 293
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
14-271 5.25e-31

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: 120.69  E-value: 5.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGG-ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd07860  82 HQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTE---GAIKLADFGLARAFGVPVRTYT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPF-WDEDQHKLYQQIKA----------GAYDFPS----- 235
Cdd:cd07860 159 HEVVTLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTRRALFpGDSEIDQLFRIFRTlgtpdevvwpGVTSMPDykpsf 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 26051218 236 PEW-----DTVTP----EAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07860 239 PKWarqdfSKVVPpldeDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
12-249 5.88e-31

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: 122.47  E-value: 5.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREarICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd05627   2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvaHIRAERD--ILVEADGAWVVKMFYSFQDKRNLYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV---- 164
Cdd:cd05627  80 IMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLkkah 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 -------------------------------QGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPP 213
Cdd:cd05627 157 rtefyrnlthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 236
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 26051218 214 FWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLI 249
Cdd:cd05627 237 FCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLI 272
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
14-270 6.16e-31

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: 120.30  E-value: 6.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVrrcvklctgheYAAKIINT------KKLSARDHQKlEREARICRLLKHSNIVRLHDS--ISEEGF 85
Cdd:cd14137   6 YTIEKVIGSGSFGVV-----------YQAKLLETgevvaiKKVLQDKRYK-NRELQIMRRLKHPNIVKLKYFfySSGEKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTggELFEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLL-ASKCKgaaVKL 155
Cdd:cd14137  74 DEVYLNLVM--EYMPETLYRVIRHYSKNKQTIPiiyvklysyQLFRGLAYLHSLGICHRDIKPQNLLVdPETGV---LKL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 156 ADFGLAIEVQgdqqawfgfAGTPG--------YLSPE-VLRKEAYGKPVDIWACGVILYILLVGYPPF---WDEDQHKLY 223
Cdd:cd14137 149 CDFGSAKRLV---------PGEPNvsyicsryYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFpgeSSVDQLVEI 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 224 ---------QQIKA-----GAYDFP---SPEWDTV-----TPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14137 220 ikvlgtptrEQIKAmnpnyTEFKFPqikPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
43-270 7.28e-31

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: 119.46  E-value: 7.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  43 KIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIV--AREYYSEADASHCIQQI 120
Cdd:cd08221  31 KEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAqqKNQLFPEEVVLWYLYQI 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 121 LEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWAC 200
Cdd:cd08221 111 VSAVSHIHKAGILHRDIKTLNIFLT---KADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAV 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 201 GVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWdtvTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd08221 188 GCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERP 254
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
9-275 1.27e-30

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: 120.55  E-value: 1.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKII----NTKKLSARDHqkleREARICRLLKHSNIVRLHDSI---- 80
Cdd:cd07855   2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTL----RELKILRHFKHDNIIAIRDILrpkv 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 -SEEGFH-YLVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADF 158
Cdd:cd07855  78 pYADFKDvYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE---LKIGDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLAIEV---QGDQQAWFG-FAGTPGYLSPEVLRK-EAYGKPVDIWACGVI---------------------LYILLVGYP 212
Cdd:cd07855 154 GMARGLctsPEEHKYFMTeYVATRWYRAPELMLSlPEYTQAIDMWSVGCIfaemlgrrqlfpgknyvhqlqLILTVLGTP 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 213 PfwdedqHKLYQQIKAG---AY--DFPSP---EWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPWVCQR 275
Cdd:cd07855 234 S------QAVINAIGADrvrRYiqNLPNKqpvPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
12-271 1.28e-30

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: 122.04  E-value: 1.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARicRLLKHSN---IVRLHDSISEEGFHYL 88
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREER--NVLVNGDcqwITTLHYAFQDENYLYL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGEL------FEDIVAreyysEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAI 162
Cdd:cd05624 150 VMDYYVGGDLltllskFEDKLP-----EDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN---GHIRLADFGSCL 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWFGFA-GTPGYLSPEVLRKE-----AYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI--KAGAYDFP 234
Cdd:cd05624 222 KMNDDGTVQSSVAvGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHEERFQFP 301
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 26051218 235 SPEWDtVTPEAKNLInQMLTINPAKRITAH---EALKHPW 271
Cdd:cd05624 302 SHVTD-VSEEAKDLI-QRLICSRERRLGQNgieDFKKHAF 339
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
14-271 2.04e-30

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: 118.74  E-value: 2.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtkkLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH---LDAEEGTPSTaiREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGG-ELFEDIVA-REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEvqgdqq 169
Cdd:cd07836  79 YMDKDlKKYMDTHGvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKR---GELKLADFGLARA------ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 awFG-----FAG---TPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPFW---DEDQHKLYQQIKAGAYD--FP- 234
Cdd:cd07836 150 --FGipvntFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPgtnNEDQLLKIFRIMGTPTEstWPg 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 235 ---SPEWDTVTPEAK----------------NLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07836 228 isqLPEYKPTFPRYPpqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
12-272 2.25e-30

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: 118.14  E-value: 2.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGElFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGDQQ 169
Cdd:cd06612  79 YCGAGS-VSDIMkiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEG---QAKLADFGVSGQLTDTMA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagayDFPSP------EWdtvTP 243
Cdd:cd06612 155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIP----NKPPPtlsdpeKW---SP 227
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06612 228 EFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
12-249 2.54e-30

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: 120.91  E-value: 2.54e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREaricrLLKHSN---IVRLHDSISEEGF 85
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEqvgHIRAERD-----ILVEADslwVVKMFYSFQDKLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ 165
Cdd:cd05628  76 LYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLCTGLK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 -----------------------------------GDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVG 210
Cdd:cd05628 153 kahrtefyrnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIG 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 26051218 211 YPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLI 249
Cdd:cd05628 233 YPPFCSETPQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
9-271 2.62e-30

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: 118.87  E-value: 2.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKLsardhqKLEREA---------RICRLLK--HSNIVRL- 76
Cdd:cd07843   2 RSVDEYEKLNRIEEGTYGVVYRARDKKTG-----EIVALKKL------KMEKEKegfpitslrEINILLKlqHPNIVTVk 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  77 -------HDSIseegfhYLVF-----DLVTggeLFEDIvaREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL 144
Cdd:cd07843  71 evvvgsnLDKI------YMVMeyvehDLKS---LMETM--KQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 145 ASKckgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF--------- 214
Cdd:cd07843 140 NNR---GILKICDFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFpgkseidql 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 215 --------------WDEdqhkLYQQIKAGAYDFPSPEWDT---------VTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07843 217 nkifkllgtptekiWPG----FSELPGAKKKTFTKYPYNQlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
2-261 2.99e-30

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: 119.72  E-value: 2.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   2 ATTVTCTRFTDeYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLER-EARICRLL-KHSNIVRLHDS 79
Cdd:cd05615   1 SNNLDRVRLTD-FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMvEKRVLALQdKPPFLTQLHSC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  80 ISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFG 159
Cdd:cd05615  80 FQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSE---GHIKIADFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 160 LAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewd 239
Cdd:cd05615 157 MCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK---- 232
                       250       260
                ....*....|....*....|..
gi 26051218 240 TVTPEAKNLINQMLTINPAKRI 261
Cdd:cd05615 233 SLSKEAVSICKGLMTKHPAKRL 254
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-282 3.81e-30

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: 120.88  E-value: 3.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVF 90
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQDDRYLYMVM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05622 153 EYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCMKMNKEGMV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFA-GTPGYLSPEVLRKEA----YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEA 245
Cdd:cd05622 229 RCDTAvGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEA 308
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAK--RITAHEALKHP--------WVCQRSTVASMM 282
Cdd:cd05622 309 KNLICAFLTDREVRlgRNGVEEIKRHLffkndqwaWETLRDTVAPVV 355
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
12-270 4.42e-30

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: 116.94  E-value: 4.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTG--HEYAAKIINTKKLSARDH-QKLEREARICRLLK-HSNIVRLHDSISEEGFHY 87
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDKLHDlyDRNKGRLVALKHIYPTSSpSRILNELECLERLGgSNNVSGLITAFRNEDQVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFdlvtggELFEDIVAREYYSE---ADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKC-KGAavkLADFGLAiE 163
Cdd:cd14019  81 AVL------PYIEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETgKGV---LVDFGLA-Q 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGD---QQAwfGFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVG-YPPFW-DEDQHKLYQQI----KAGAYDf 233
Cdd:cd14019 151 REEDrpeQRA--PRAGTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGrFPFFFsSDDIDALAEIAtifgSDEAYD- 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 234 pspewdtvtpeaknLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14019 228 --------------LLDKLLELDPSKRITAEEALKHP 250
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
20-271 4.76e-30

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: 118.86  E-value: 4.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRLLK-HSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVL--KKdviLQDDDVECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFA 175
Cdd:cd05590  81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHE---GHCKLADFGMCKEGIFNGKTTSTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpeWdtVTPEAKNLINQMLTI 255
Cdd:cd05590 158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPT--W--LSQDAVDILKAFMTK 233
                       250       260
                ....*....|....*....|..
gi 26051218 256 NPAKRITA------HEALKHPW 271
Cdd:cd05590 234 NPTMRLGSltlggeEAILRHPF 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
5-271 5.28e-30

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: 118.57  E-value: 5.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   5 VTCTRFTDeYQLYEDIGKGAFSVVRRCVKLCTGHEYAAK-IINtkkLSARD--HQKLEREARICRLLKHSNIVRLHDSIS 81
Cdd:cd07866   2 YGCSKLRD-YEILGKLGEGTFGEVYKARQIKTGRVVALKkILM---HNEKDgfPITALREIKILKKLKHPNVVPLIDMAV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 EEG-------------FHYLVFDLvTGgeLFEDivAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKc 148
Cdd:cd07866  78 ERPdkskrkrgsvymvTPYMDHDL-SG--LLEN--PSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQ- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 149 kgAAVKLADFGLAIEVQGDQQAWfGFAGTPG------------YLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF- 214
Cdd:cd07866 152 --GILKIADFGLARPYDGPPPNP-KGGGGGGtrkytnlvvtrwYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPILq 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 215 --WDEDQ-HKLY-------QQIKAGAYDFPS-PEWDTVT--------------PEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd07866 229 gkSDIDQlHLIFklcgtptEETWPGWRSLPGcEGVHSFTnyprtleerfgklgPEGLDLLSKLLSLDPYKRLTASDALEH 308

                ..
gi 26051218 270 PW 271
Cdd:cd07866 309 PY 310
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
20-261 6.80e-30

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: 118.36  E-value: 6.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVL--KKdviLQDDDVDCTMTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFA 175
Cdd:cd05591  81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE---GHCKLADFGMCKEGILNGKTTTTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGayDFPSPEWdtVTPEAKNLINQMLTI 255
Cdd:cd05591 158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYPVW--LSKEAVSILKAFMTK 233

                ....*.
gi 26051218 256 NPAKRI 261
Cdd:cd05591 234 NPAKRL 239
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
13-271 7.30e-30

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: 117.52  E-value: 7.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDH---QKLEREARICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI---RLESEEEgvpSTAIREISLLKELQHPNIVCLEDVLMQENRLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGG--ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGD 167
Cdd:cd07861  78 FEFLSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADFGLARAFGIP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFW-DEDQHKLY----------QQIKAGAYDFPS 235
Cdd:cd07861 155 VRVYTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHgDSEIDQLFrifrilgtptEDIWPGVTSLPD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 236 -----PEW--DTVTPEAKN-------LINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07861 235 ykntfPKWkkGSLRTAVKNldedgldLLEKMLIYDPAKRISAKKALVHPY 284
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
14-269 7.77e-30

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: 117.40  E-value: 7.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDHQKL-EREARICRLLKHSNIVRLHDS--ISEEGFH---Y 87
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKI---LCHSKEDVKEaMREIENYRLFNHPNILRLLDSqiVKEAGGKkevY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQM---GVVHRDLKPENLLLASKckGAAVkLADFGL 160
Cdd:cd13986  79 LLLPYYKRGSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSED--DEPI-LMDLGS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 A----IEVQGDQQA-----WFGFAGTPGYLSPEVLRKEAYG---KPVDIWACGVILYILLVGYPPFWDEDQH--KLYQQI 226
Cdd:cd13986 156 MnparIEIEGRREAlalqdWAAEHCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFERIFQKgdSLALAV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 26051218 227 KAGAYDFPSPEwdTVTPEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd13986 236 LSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
13-261 1.73e-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: 115.89  E-value: 1.73e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKiintkKLSARDHQKLE---REARIC-RLLKHSNIVRLHDS--ISEEGfh 86
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALK-----RMYFNDEEQLRvaiKEIEIMkRLCGHPNIVQYYDSaiLSSEG-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVT---GGELFEDIVARE--YYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASkckGAAVKLADFG 159
Cdd:cd13985  74 RKEVLLLMeycPGSLVDILEKSPpsPLSEEEVLRIFYQICQAVghLHSQSPPIIHRDIKIENILFSN---TGRFKLCDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 160 LAIEVQGDQQAWFGFA---------GTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFwdEDQHKLyqQIK 227
Cdd:cd13985 151 SATTEHYPLERAEEVNiieeeiqknTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF--DESSKL--AIV 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 228 AGAYdfPSPEWDTVTPEAKNLINQMLTINPAKRI 261
Cdd:cd13985 227 AGKY--SIPEQPRYSPELHDLIRHMLTPDPAERP 258
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
14-270 2.20e-29

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: 116.28  E-value: 2.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE-REARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05630  82 MNGGDLKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLAVHVPEGQTI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLIN 250
Cdd:cd05630 159 K-GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCS 237
                       250       260
                ....*....|....*....|....*
gi 26051218 251 QMLTINPAKRI-----TAHEALKHP 270
Cdd:cd05630 238 MLLCKDPAERLgcrggGAREVKEHP 262
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
103-269 3.35e-29

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: 115.58  E-value: 3.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 103 VAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYL 181
Cdd:cd13974 123 VIREKrLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVL--NKRTRKITITNFCLGKHLVSEDDLLKDQRGSPAYI 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 182 SPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewDTVTPEAKNLINQMLTINPAKR 260
Cdd:cd13974 201 SPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKR 278

                ....*....
gi 26051218 261 ITAHEALKH 269
Cdd:cd13974 279 LTASEVLDS 287
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
11-272 4.98e-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: 114.55  E-value: 4.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCV--KLCTGHEYAAKIINTkklsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd14112   2 TGRFSFGSEIFRGRFSVIVKAVdsTTETDAHCAVKIFEV----SDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDlvtggELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKcKGAAVKLADFGLAIEV 164
Cdd:cd14112  78 VME-----KLQEDVftrfSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRAQKV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGD----QQAWFGFAgtpgylSPEVLRKEAYGKP-VDIWACGVILYILLVGYPPFWDE--DQHKLYQQIKAGAYDfPSPE 237
Cdd:cd14112 152 SKLgkvpVDGDTDWA------SPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCR-PNLI 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 238 WDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14112 225 FVEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
14-274 5.08e-29

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 118.82  E-value: 5.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhqKLEREARICRLLK--HSNIVRLH------DSISEEGF 85
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEAD--KNRAQAEVCCLLNcdFFSIVKCHedfakkDPRNPENV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   86 HY--LVFDLVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFG 159
Cdd:PTZ00283 112 LMiaLVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL---CSNGLVKLGDFG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  160 L----AIEVQGDQQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDfPS 235
Cdd:PTZ00283 189 FskmyAATVSDDVGR--TFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYD-PL 265
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 26051218  236 PewDTVTPEAKNLINQMLTINPAKRITAHEALKHPwVCQ 274
Cdd:PTZ00283 266 P--PSISPEMQEIVTALLSSDPKRRPSSSKLLNMP-ICK 301
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
15-260 5.92e-29

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 114.17  E-value: 5.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     15 QLYEDIGKGAFSVVRRCV-KLCTGHEY---AAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKKKvevAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     91 DLVTGGELFEDIVA-REYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQ 169
Cdd:smart00219  81 EYMEGGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRDLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    170 ----------AWfgfagtpgyLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEw 238
Cdd:smart00219 158 yrkrggklpiRW---------MAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNG-YRLPQPP- 226
                          250       260
                   ....*....|....*....|..
gi 26051218    239 dTVTPEAKNLINQMLTINPAKR 260
Cdd:smart00219 227 -NCPPELYDLMLQCWAEDPEDR 247
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
9-269 5.95e-29

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: 114.77  E-value: 5.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARDH--QKLEREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd14046   3 RYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKI---KLRSESKnnSRILREVMLLSRLNHQHVVRYYQAWIERANL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV-- 164
Cdd:cd14046  80 YIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSN---GNVKIGDFGLATSNkl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 ----------------QGDQQAWFGFAGTPGYLSPEVL--RKEAYGKPVDIWACGVILYILLvgYPPFWDEDQHKLYQQI 226
Cdd:cd14046 157 nvelatqdinkstsaaLGSSGDLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMC--YPFSTGMERVQILTAL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 26051218 227 KAGAYDFPsPEWDTVT-PEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd14046 235 RSVSIEFP-PDFDDNKhSKQAKLIRWLLNHDPAKRPSAQELLKS 277
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
42-271 7.78e-29

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 115.85  E-value: 7.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   42 AKIINTKKLsarDHQKLEReaRICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQIL 121
Cdd:PTZ00426  67 SKIIKQKQV---DHVFSER--KILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  122 EAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQqawFGFAGTPGYLSPEVLRKEAYGKPVDIWACG 201
Cdd:PTZ00426 142 LIFEYLQSLNIVYRDLKPENLLLD---KDGFIKMTDFGFAKVVDTRT---YTLCGTPEYIAPEILLNVGHGKAADWWTLG 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218  202 VILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSpewdTVTPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:PTZ00426 216 IFIYEILVGCPPFYANEPLLIYQKILEGIIYFPK----FLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPW 286
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-269 9.05e-29

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: 114.20  E-value: 9.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   8 TRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAK-IINTKKLSARDhqKLEREARICRLLKHSNIVRLHDSISE---E 83
Cdd:cd14048   2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELARE--KVLREVRALAKLDHPGIVRYFNAWLErppE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFH--------YLVFDLVTGGELFEDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAA 152
Cdd:cd14048  80 GWQekmdevylYIQMQLCRKENLKDWMNRRCTMESRELFVClniFKQIASAVEYLHSKGLIHRDLKPSNVFFSLD---DV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 153 VKLADFGLA---------IEVQGDQQAW---FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYppfwDEDQH 220
Cdd:cd14048 157 VKVGDFGLVtamdqgepeQTVLTPMPAYakhTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSF----STQME 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 221 KLYQQIKAGAYDFPsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd14048 233 RIRTLTDVRKLKFP-ALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
20-272 1.13e-28

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: 114.37  E-value: 1.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVrrCVklcTGHEYAAKIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd06658  30 IGEGSTGIV--CI---ATEKHTGKQVAVKKMDLRKQQRREllfNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd06658 105 AL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR---IKLSDFGFCAQVSKEVPKRKSLVG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKagayDFPSP---EWDTVTPEAKNLINQML 253
Cdd:cd06658 181 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIR----DNLPPrvkDSHKVSSVLRGFLDLML 256
                       250
                ....*....|....*....
gi 26051218 254 TINPAKRITAHEALKHPWV 272
Cdd:cd06658 257 VREPSQRATAQELLQHPFL 275
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
20-270 1.14e-28

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: 114.23  E-value: 1.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLER-EARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAvKLADFGLAIEVQGDQQAwFGFAG 176
Cdd:cd05607  90 KYHIynVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLL--DDNGNC-RLSDLGLAVEVKEGKPI-TQRAG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAY-DFPSPEWDTVTPEAKNLINQMLTI 255
Cdd:cd05607 166 TNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLeDEVKFEHQNFTEEAKDICRLFLAK 245
                       250
                ....*....|....*
gi 26051218 256 NPAKRITAHEALKHP 270
Cdd:cd05607 246 KPENRLGSRTNDDDP 260
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
12-267 1.73e-28

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: 113.25  E-value: 1.73e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCvkLCTGHEYAAKIINTKKLSARDHQKLEREARICRLlKHSNIVRL---HDSISEEGFHYL 88
Cdd:cd13979   3 EPLRLQEPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVlaaETGTDFASLGLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIvaREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQ 165
Cdd:cd13979  80 IMEYCGNGTLQQLI--YEGSEPLPLAHRILislDIARALRFCHSHGIVHLDVKPANILI---SEQGVCKLCDFGCSVKLG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GD---QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAY-DFPSPEWDTV 241
Cdd:cd13979 155 EGnevGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRpDLSGLEDSEF 234
                       250       260
                ....*....|....*....|....*.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEAL 267
Cdd:cd13979 235 GQRLRSLISRCWSAQPAERPNADESL 260
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
12-271 2.80e-28

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: 112.85  E-value: 2.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKL--SARD---HQKLEREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd07847   1 EKYEKLSKIGEGSYGVVFKCRNRETG-----QIVAIKKFveSEDDpviKKIALREIRMLKQLKHPNLVNLIEVFRRKRKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEdivaREYYSEADASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI 162
Cdd:cd07847  76 HLVFEYCDHTVLNE----LEKNPRGVPEHLIKkiiwQTLQAVNFCHKHNCIHRDVKPENILIT---KQGQIKLCDFGFAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWFGFAGTPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVGyPPFW----DEDQhkLY-------------Q 224
Cdd:cd07847 149 ILTGPGDDYTDYVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTG-QPLWpgksDVDQ--LYlirktlgdliprhQ 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 225 QIKAGAYDF-----PSPE--------WDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07847 226 QIFSTNQFFkglsiPEPEtrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-272 2.82e-28

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: 112.14  E-value: 2.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSIS-EEGFHYLVFD 91
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEgEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd08223  81 FCEGGDLYTRLKEQkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLGIARVLESSSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL-YQQIKAGAYDFPSpewdTVTPEAKNL 248
Cdd:cd08223 158 MATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLvYKILEGKLPPMPK----QYSPELGEL 233
                       250       260
                ....*....|....*....|....
gi 26051218 249 INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd08223 234 IKAMLHQDPEKRPSVKRILRQPYI 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
16-260 3.31e-28

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: 112.26  E-value: 3.31e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     16 LYEDIGKGAFSVVRRCVKLCTGHEY----AAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDA-SEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     92 LVTGGELFEDIVAREYY--SEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQ 169
Cdd:smart00221  82 YMPGGDLLDYLRKNRPKelSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRDLYDDDY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    170 ----------AWfgfagtpgyLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEw 238
Cdd:smart00221 159 ykvkggklpiRW---------MAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKG-YRLPKPP- 227
                          250       260
                   ....*....|....*....|..
gi 26051218    239 dTVTPEAKNLINQMLTINPAKR 260
Cdd:smart00221 228 -NCPPELYKLMLQCWAEDPEDR 248
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
13-263 3.40e-28

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: 111.99  E-value: 3.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPK-SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQA 170
Cdd:cd08219  80 CDGGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLTSPGAY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYdfpSPEWDTVTPEAKNLIN 250
Cdd:cd08219 157 ACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSY---KPLPSHYSYELRSLIK 233
                       250
                ....*....|...
gi 26051218 251 QMLTINPAKRITA 263
Cdd:cd08219 234 QMFKRNPRSRPSA 246
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
12-272 3.91e-28

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: 113.93  E-value: 3.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAakiinTKKLSaRDHQKLE------REARICRLLKHSNIVRLHD----SIS 81
Cdd:cd07851  15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVA-----IKKLS-RPFQSAIhakrtyRELRLLKHMKHENVIGLLDvftpASS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 EEGFH--YLVFDLVtGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFG 159
Cdd:cd07851  89 LEDFQdvYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCE---LKILDFG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 160 LAieVQGDQQAwFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI------------ 226
Cdd:cd07851 164 LA--RHTDDEM-TGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRImnlvgtpdeell 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 227 ------KAGAY-----DFPSPEWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07851 241 kkisseSARNYiqslpQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
12-270 4.19e-28

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: 112.78  E-value: 4.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCvklctGHEYAAKIINTKKLsaRDHQKLE-------REARICRLLKHSNIVRLHDSISEEG 84
Cdd:cd07848   1 NKFEVLGVVGEGAYGVVLKC-----RHKETKEIVAIKKF--KDSEENEevkettlRELKMLRTLKQENIVELKEAFRRRG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGG--ELFEDI-------VAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKL 155
Cdd:cd07848  74 KLYLVFEYVEKNmlELLEEMpngvppeKVRSY---------IYQLIKAIHWCHKNDIVHRDIKPENLLISHN---DVLKL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 156 ADFGLAIEV-QGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDE----------------- 217
Cdd:cd07848 142 CDFGFARNLsEGSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGEseidqlftiqkvlgplp 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 218 -DQHKL-YQQIKAGAYDFPS---PE------WDTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd07848 222 aEQMKLfYSNPRFHGLRFPAvnhPQslerryLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
13-271 5.67e-28

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: 112.36  E-value: 5.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKiiNTKKLSARDHQKLE--REARICRLLK---HSNIVRLHDSIS-----E 82
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALK--SVRVQTNEDGLPLStvREVALLKRLEafdHPNIVRLMDVCAtsrtdR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTggelfEDIvaREYYSEADA--------SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVK 154
Cdd:cd07863  79 ETKVTLVFEHVD-----QDL--RTYLDKVPPpglpaetiKDLMRQFLRGLDFLHANCIVHRDLKPENILVTS---GGQVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 155 LADFGLAiEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYIL---------------------LVGYPP 213
Cdd:cd07863 149 LADFGLA-RIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMfrrkplfcgnseadqlgkifdLIGLPP 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 214 fwdEDQHKLYQQIKAGAYDFPSPE-WDTVTPE----AKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07863 228 ---EDDWPRDVTLPRGAFSPRGPRpVQSVVPEieesGAQLLLEMLTFNPHKRISAFRALQHPF 287
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
11-272 5.89e-28

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: 112.14  E-value: 5.89e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklsarDHQKLER---EARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd06611   4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE-----SEEELEDfmvEIDILSECKHPNIVGLYEAYFYENKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREY-YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQG 166
Cdd:cd06611  79 ILIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADFGVSAKNKS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVL-----RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGaydfPSPEWDTV 241
Cdd:cd06611 156 TLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKS----EPPTLDQP 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 242 ---TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06611 232 skwSSSFNDFLKSCLVKDPDDRPTAAELLKHPFV 265
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
20-261 6.26e-28

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: 112.86  E-value: 6.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRL-LKHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKAL--KKdvvLEDDDVECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAaVKLADFGLAIE-VQGDQQAwFGF 174
Cdd:cd05592  81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL--DREGH-IKIADFGMCKEnIYGENKA-STF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFpsPEWdtVTPEAKNLINQMLT 254
Cdd:cd05592 157 CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHY--PRW--LTKEAASCLSLLLE 232

                ....*..
gi 26051218 255 INPAKRI 261
Cdd:cd05592 233 RNPEKRL 239
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
20-270 7.13e-28

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: 111.37  E-value: 7.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK----LEREARICRLLKHSNIVRLHDSiSEEGFHYLVF-DLVT 94
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEvveaIREEIRMMARLNHPNIVRMLGA-TQHKSHFNIFvEWMA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGE---LFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckGAAVKLADFGLAI--------- 162
Cdd:cd06630  87 GGSvasLLSKYGA---FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDST--GQRLRIADFGAAArlaskgtga 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 -EVQGDqqawfgFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPfWDEDQHKLYQQI--KAGAYDFPSPEWD 239
Cdd:cd06630 162 gEFQGQ------LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPP-WNAEKISNHLALifKIASATTPPPIPE 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 240 TVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd06630 235 HLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
12-274 1.08e-27

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: 112.83  E-value: 1.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHD------SISEEGF 85
Cdd:cd07877  17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDvftparSLEEFND 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVtGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQ 165
Cdd:cd07877  97 VYLVTHLM-GADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE---LKILDFGLARHTD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQawfGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI------------------ 226
Cdd:cd07877 172 DEMT---GYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLIlrlvgtpgaellkkisse 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 227 KAGAY-----DFPSPEWDTV----TPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd07877 249 SARNYiqsltQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
12-271 1.69e-27

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: 110.97  E-value: 1.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCvklctGHEYAAKIINTKKLSARDHQKL-----EREARICRLLKHSNIVRLHDSISEEGFH 86
Cdd:cd07846   1 EKYENLGLVGEGSYGMVMKC-----RHKETGQIVAIKKFLESEDDKMvkkiaMREIKMLKQLRHENLVNLIEVFRRKKRW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQG 166
Cdd:cd07846  76 YLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF-WDEDQHKLYQQIK----------------- 227
Cdd:cd07846 153 PGEVYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFpGDSDIDQLYHIIKclgnliprhqelfqknp 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 26051218 228 --AGAY--DFPSPE-----WDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07846 233 lfAGVRlpEVKEVEplerrYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
20-272 1.88e-27

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: 110.32  E-value: 1.88e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQK-------LEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRkksmldaLQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ------G 166
Cdd:cd06628  88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNK---GGIKISDFGISKKLEanslstK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQhklYQQI-KAGAYDFPSPEwDTVTPEA 245
Cdd:cd06628 165 NNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIfKIGENASPTIP-SNISSEA 240
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06628 241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
12-270 1.92e-27

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: 111.09  E-value: 1.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKII-NTKKlsardhQKLEREARICRLLK-HSNIVRLHDSISEE--GFHY 87
Cdd:cd14132  18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkPVKK------KKIKREIKILQNLRgGPNIVKLLDVVKDPqsKTPS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLV------TGGELFEDIVAREYyseadashcIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLADFGLA 161
Cdd:cd14132  92 LIFEYVnntdfkTLYPTLTDYDIRYY---------MYELLKALDYCHSKGIMHRDVKPHNIMIDHEKR--KLRLIDWGLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 iEvqgdqqawFGFAGTP--------GYLSPEVL---RKEAYGkpVDIWACGVILYILLVGYPPFW----DEDQ------- 219
Cdd:cd14132 161 -E--------FYHPGQEynvrvasrYYKGPELLvdyQYYDYS--LDMWSLGCMLASMIFRKEPFFhghdNYDQlvkiakv 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 220 --------------HKLYQQIKAGAYDFPSPEWDT---------VTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14132 230 lgtddlyayldkygIELPPRLNDILGRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
13-271 2.48e-27

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: 110.92  E-value: 2.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDHQKLE--REARICRLLKHSNIVRLH--------DSIse 82
Cdd:cd07845   8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISslREITLLLNLRHPNIVELKevvvgkhlDSI-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 egfhYLVF-----DLvtgGELFEDIVAReyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLAD 157
Cdd:cd07845  84 ----FLVMeyceqDL---ASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLAiEVQGDQQAWFgfagTPG-----YLSPEVL-RKEAYGKPVDIWACGVILYILLVGYPPF----------------- 214
Cdd:cd07845 152 FGLA-RTYGLPAKPM----TPKvvtlwYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLpgkseieqldliiqllg 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 215 ------W-DEDQHKLYQQI--KAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07845 227 tpnesiWpGFSDLPLVGKFtlPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
6-272 2.64e-27

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: 111.12  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   6 TCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKII----NTKKLSARDHqkleREARICRLLKHSNIVRLHDS-I 80
Cdd:cd07856   4 TVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKImkpfSTPVLAKRTY----RELKLLKHLRHENIISLSDIfI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVtGGELFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGL 160
Cdd:cd07856  80 SPLEDIYFVTELL-GTDLHRLLTSRPLEKQF-IQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCD---LKICDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AiEVQGDQQAwfGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFP----- 234
Cdd:cd07856 155 A-RIQDPQMT--GYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPddvin 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 235 ----------------------SPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07856 232 ticsentlrfvqslpkrervpfSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
14-272 3.06e-27

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: 111.34  E-value: 3.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVrrCVKLCTGHEYAAKI-------INTKKLSARdhqKLEREARICRLLK-HSNIVRLHDS--ISEE 83
Cdd:cd07857   2 YELIKELGQGAYGIV--CSARNAETSEEETVaikkitnVFSKKILAK---RALRELKLLRHFRgHKNITCLYDMdiVFPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFH--YLVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA 161
Cdd:cd07857  77 NFNelYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCE---LKICDFGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 I---EVQGDQQAWF-GFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ-HKLYQ----------- 224
Cdd:cd07857 153 RgfsENPGENAGFMtEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYvDQLNQilqvlgtpdee 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 225 ------QIKAGAYDFPSPEWDTV---------TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07857 233 tlsrigSPKAQNYIRSLPNIPKKpfesifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
18-271 3.38e-27

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: 110.05  E-value: 3.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTgge 97
Cdd:cd07870   6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 lfEDIVarEYYSEADA---SHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLAskCKGAaVKLADFGLAIEVQGDQQA 170
Cdd:cd07870  82 --TDLA--QYMIQHPGglhPYNVRlfmfQLLRGLAYIHGQHILHRDLKPQNLLIS--YLGE-LKLADFGLARAKSIPSQT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFWD-----EDQHKLY-------QQIKAGAYDFPS-- 235
Cdd:cd07870 155 YSSEVVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGvsdvfEQLEKIWtvlgvptEDTWPGVSKLPNyk 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 26051218 236 PEWDTVT---------------PEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07870 235 PEWFLPCkpqqlrvvwkrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPY 285
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
12-271 4.00e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.91  E-value: 4.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   12 DEYQLYEDIGKGAFSVVRRcvklcTGHEYAAKIINTKKLsaRDHQKLE-------REARICRLLKHSNIVRLHDSISEEG 84
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYK-----ARDRVTNETIALKKI--RLEQEDEgvpstaiREISLLKEMQHGNIVRLQDVVHSEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   85 FHYLVFdlvtggELFEDIVAREYYSEADAS---HCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLAD 157
Cdd:PLN00009  75 RLYLVF------EYLDLDLKKHMDSSPDFAknpRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN--ALKLAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  158 FGLAIEVQGDQQAWFGFAGTPGYLSPEVLR-KEAYGKPVDIWACGVIlYILLVGYPPFWDEDQ-----HKLYQ------- 224
Cdd:PLN00009 147 FGLARAFGIPVRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCI-FAEMVNQKPLFPGDSeidelFKIFRilgtpne 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218  225 QIKAGAYDFPS-----PEWD---------TVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:PLN00009 226 ETWPGVTSLPDyksafPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1-273 4.12e-27

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 109.18  E-value: 4.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    1 MATTVT-CTRFTDEYQLYEDIG--KGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQklerearicrLLK-HSNI 73
Cdd:PHA03390   2 MDKSLSeLVQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEpmvHQ----------LMKdNPNF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   74 VRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQmgVVHRDLKPENLLL-ASKCKg 150
Cdd:PHA03390  72 IKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALndLHKHN--IIHNDIKLENVLYdRAKDR- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  151 aaVKLADFGLAIEVqgdqqawfgfaGTPG-------YLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWD------- 216
Cdd:PHA03390 149 --IYLCDYGLCKII-----------GTPScydgtldYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEdedeeld 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218  217 -EDQHKLYQQikagayDFPSPEwdTVTPEAKNLINQMLTINPAKRITAHEA-LKHPWVC 273
Cdd:PHA03390 216 lESLLKRQQK------KLPFIK--NVSKNANDFVQSMLKYNINYRLTNYNEiIKHPFLK 266
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
18-271 5.63e-27

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: 108.85  E-value: 5.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF--DLVTG 95
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELfedivaREYYSEADA-------SHCIqQILEAV--LHCHQMGVVHRDLKPENLLLaskcKGAA--VKLADFGLAIEV 164
Cdd:cd13983  87 GTL------KQYLKRFKRlklkvikSWCR-QILEGLnyLHTRDPPIIHRDLKCDNIFI----NGNTgeVKIGDLGLATLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDqqawfgFA----GTPGYLSPEVLrKEAYGKPVDIWACGVILYILLVG-YPpfWDEDQH------KLYQQIKAGAYDf 233
Cdd:cd13983 156 RQS------FAksviGTPEFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGeYP--YSECTNaaqiykKVTSGIKPESLS- 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26051218 234 pspewDTVTPEAKNLINQMLTInPAKRITAHEALKHPW 271
Cdd:cd13983 226 -----KVKDPELKDFIEKCLKP-PDERPSARELLEHPF 257
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
12-271 6.19e-27

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: 109.54  E-value: 6.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFsvvrrcvklctGHEYAAKIINTKKLSARDHQKLE-----------REARICRLLKHSN-IVRLHD- 78
Cdd:cd07837   1 DAYEKLEKIGEGTY-----------GKVYKARDKNTGKLVALKKTRLEmeeegvpstalREVSLLQMLSQSIyIVRLLDv 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  79 -SISEEG--FHYLVFD-LVTGGELFEDIVAREYYSEADAShCIQ----QILEAVLHCHQMGVVHRDLKPENLLLaSKCKG 150
Cdd:cd07837  70 eHVEENGkpLLYLVFEyLDTDLKKFIDSYGRGPHNPLPAK-TIQsfmyQLCKGVAHCHSHGVMHRDLKPQNLLV-DKQKG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 151 aAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF-WDEDQHKLY----- 223
Cdd:cd07837 148 -LLKIADLGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFpGDSELQQLLhifrl 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 224 -----QQIKAGAYDFPS----PEWD---------TVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07837 227 lgtpnEEVWPGVSKLRDwheyPQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
20-277 9.79e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 110.30  E-value: 9.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  100 ediVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGFAGTPG 179
Cdd:PLN00034 160 ---EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRILAQTMDPCNSSVGTIA 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  180 YLSPEV----LRKEAY-GKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLT 254
Cdd:PLN00034 234 YMSPERintdLNHGAYdGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATASREFRHFISCCLQ 313
                        250       260
                 ....*....|....*....|...
gi 26051218  255 INPAKRITAHEALKHPWVCQRST 277
Cdd:PLN00034 314 REPAKRWSAMQLLQHPFILRAQP 336
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
12-271 9.96e-27

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: 110.04  E-value: 9.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHD----SISEEGFH- 86
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDvftpDLSLDRFHd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 -YLVFDLVtgGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQ 165
Cdd:cd07880  95 fYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE---LKILDFGLARQTD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQawfGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ-------------------HKLyQQ 225
Cdd:cd07880 170 SEMT---GYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHldqlmeimkvtgtpskefvQKL-QS 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 226 IKAGAYDFPSPEWD---------TVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07880 246 EDAKNYVKKLPRFRkkdfrsllpNANPLAVNVLEKMLVLDAESRITAAEALAHPY 300
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-282 1.19e-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: 110.47  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVF 90
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPwVVQLFCAFQDDKYLYMVM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05621 132 EYMPGGDLV-NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD---KYGHLKLADFGTCMKMDETGMV 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFA-GTPGYLSPEVLRKEA----YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEA 245
Cdd:cd05621 208 HCDTAvGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISKHA 287
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAK--RITAHEALKHP--------WVCQRSTVASMM 282
Cdd:cd05621 288 KNLICAFLTDREVRlgRNGVEEIKQHPffrndqwnWDNIRETAAPVV 334
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
20-272 1.52e-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: 107.85  E-value: 1.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH---QK-----LEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRAdsrQKtvvdaLKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEdiVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGL---AIEVQG 166
Cdd:cd06629  89 YVPGGSIGS--CLRKYgkFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDL---EGICKISDFGIskkSDDIYG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAwFGFAGTPGYLSPEVL--RKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ----HKLYQQIKAGaydfPSPEWDT 240
Cdd:cd06629 164 NNGA-TSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAiaamFKLGNKRSAP----PVPEDVN 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 241 VTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06629 239 LSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
9-269 1.59e-26

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: 107.58  E-value: 1.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkKLSARdhqKLEREARICRLLKHSNIVRLH----------- 77
Cdd:cd14047   3 RFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV---KLNNE---KAEREVKALAKLDHPNIVRYNgcwdgfdydpe 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  78 -----DSISEEGFHYLVFDLVTGGELfEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCK 149
Cdd:cd14047  77 tsssnSSRSKTKCLFIQMEFCEKGTL-ESWIEKRNGEKLDkvlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 150 gaaVKLADFGLAIEVQGDQQAWFGfAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLvgyppfWDEDQH----KLYQQ 225
Cdd:cd14047 156 ---VKIGDFGLVTSLKNDGKRTKS-KGTLSYMSPEQISSQDYGKEVDIYALGLILFELL------HVCDSAfeksKFWTD 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 26051218 226 IKAGayDFPsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd14047 226 LRNG--ILP-DIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
20-271 2.39e-26

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: 108.14  E-value: 2.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCV--KLCTGHEYAAKIINTKK-----LSardhQKLEREARICRLLKHSNIVRLHDSI--SEEGFHYLVF 90
Cdd:cd07842   8 IGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKeqytgIS----QSACREIALLRELKHENVVSLVEVFleHADKSVYLLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DlvtggelfedivareyYSEADASHCIQ--------------------QILEAVLHCHQMGVVHRDLKPENLLLASKCK- 149
Cdd:cd07842  84 D----------------YAEHDLWQIIKfhrqakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANILVMGEGPe 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 150 GAAVKLADFGLAIEVQGDQQAWFGFAG---TPGYLSPEVL---RKeaYGKPVDIWACGVILYILLVGYPPFW-------- 215
Cdd:cd07842 148 RGVVKIGDLGLARLFNAPLKPLADLDPvvvTIWYRAPELLlgaRH--YTKAIDIWAIGCIFAELLTLEPIFKgreakikk 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 216 -------------------DEDQ----------HKLYQQIKAGAYDFPSP-----EWDTVTPEAKNLINQMLTINPAKRI 261
Cdd:cd07842 226 snpfqrdqlerifevlgtpTEKDwpdikkmpeyDTLKSDTKASTYPNSLLakwmhKHKKPDSQGFDLLRKLLEYDPTKRI 305
                       330
                ....*....|
gi 26051218 262 TAHEALKHPW 271
Cdd:cd07842 306 TAEEALEHPY 315
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
15-262 2.87e-26

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 106.81  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    15 QLYEDIGKGAFSVVRRCV--KLCTGHEY--AAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkGEGENTKIkvAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    91 DLVTGGELfedivaREY-------YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIE 163
Cdd:pfam07714  81 EYMPGGDL------LDFlrkhkrkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV---VKISDFGLSRD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   164 VQGDQQAwfgFAGTPGYL-----SPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:pfam07714 152 IYDDDYY---RKRGGGKLpikwmAPESLKDGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLEDG-YRLPQPE 227
                         250       260
                  ....*....|....*....|....*
gi 26051218   238 wdTVTPEAKNLINQMLTINPAKRIT 262
Cdd:pfam07714 228 --NCPDELYDLMKQCWAYDPEDRPT 250
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
14-272 2.87e-26

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: 108.02  E-value: 2.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKH------SNIVRLHDSISEEGFHY 87
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKK---RFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEVq 165
Cdd:cd14210  92 IVFELL-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSK-SSIKVIDFGSSCFE- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQ-----QAWFgfagtpgYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQH---------------KLYQQ 225
Cdd:cd14210 169 GEKvytyiQSRF-------YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEeqlacimevlgvppkSLIDK 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 226 IKAGAYDF-----PSPEWDTV----TPEAKNL--------------INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14210 242 ASRRKKFFdsngkPRPTTNSKgkkrRPGSKSLaqvlkcddpsfldfLKKCLRWDPSERMTPEEALQHPWI 311
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
12-271 2.88e-26

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: 108.14  E-value: 2.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE-REARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05632   2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMAlNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV-QGD 167
Cdd:cd05632  82 TIMNGGDLKFHIynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDY---GHIRISDLGLAVKIpEGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd05632 159 SIR--GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKS 236
                       250       260
                ....*....|....*....|....*....
gi 26051218 248 LINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05632 237 ICKMLLTKDPKQRLgcqeeGAGEVKRHPF 265
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
14-304 4.01e-26

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: 108.33  E-value: 4.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSI---SEEGFH--YL 88
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppSRREFKdiYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVtGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQ 168
Cdd:cd07859  82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCK---LKICDFGLARVAFNDT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QA---WFGFAGTPGYLSPEVLRK--EAYGKPVDIWACGVILYILLVGYPPFWDEDQ-HKL-----------------YQQ 225
Cdd:cd07859 158 PTaifWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVvHQLdlitdllgtpspetisrVRN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 226 IKAGAY------DFPSP---EWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNA 296
Cdd:cd07859 238 EKARRYlssmrkKQPVPfsqKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPSAQPITKLEFEFER 317

                ....*...
gi 26051218 297 RRKLKGAI 304
Cdd:cd07859 318 RRLTKEDV 325
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
20-273 5.10e-26

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: 106.75  E-value: 5.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN-----IVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGgdcpfIVCMTYAFQTPDKLCFILDLMN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIEVQGDQQAwfGF 174
Cdd:cd05606  82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLACDFSKKKPH--AS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPFWD---EDQHKLYQQIKAGAYDFPspewDTVTPEAKNLIN 250
Cdd:cd05606 157 VGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQhktKDKHEIDRMTLTMNVELP----DSFSPELKSLLE 232
                       250       260
                ....*....|....*....|....*...
gi 26051218 251 QMLTINPAKRI-----TAHEALKHPWVC 273
Cdd:cd05606 233 GLLQRDVSKRLgclgrGATEVKEHPFFK 260
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
12-274 6.30e-26

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: 107.83  E-value: 6.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHD----SISEEGFH- 86
Cdd:cd07878  15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDvftpATSIENFNe 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 -YLVFDLVtGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAieVQ 165
Cdd:cd07878  95 vYLVTNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE---LRILDFGLA--RQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAwFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDE---DQHKLYQQIkAGAydfPSPE---- 237
Cdd:cd07878 168 ADDEM-TGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNdyiDQLKRIMEV-VGT---PSPEvlkk 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 238 ------------------------WDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd07878 243 isseharkyiqslphmpqqdlkkiFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
13-272 7.68e-26

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: 105.70  E-value: 7.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSA----RDHQKLEREARICRLL----KHSNIVRLHDSI-SEE 83
Cdd:cd14101   1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFeIPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFhYLVFDL-VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAI 162
Cdd:cd14101  81 GF-LLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV--DLRTGDIKLIDFGSGA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQgdQQAWFGFAGTPGYLSPE-VLRKEAYGKPVDIWACGVILYILLVGYPPFwDEDqhklyQQIKAGAYDFPSPewdtV 241
Cdd:cd14101 158 TLK--DSMYTDFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPF-ERD-----TDILKAKPSFNKR----V 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14101 226 SNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-267 1.06e-25

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: 110.70  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218     36 TGHEYAAKIINTKKLS-ARDHQKLEREARICRLLKHSNIVRLHDS-ISEEGFHYLVFDLVTGGELFEDIVAREYYSEADA 113
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    114 SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFG-------FAGTPGYLSPEVL 186
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVAtltrtteVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    187 RKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIkaGAYDFPSPEWDTVTPEAKnLINQMLTINPAKRITAHE 265
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQL--SPVDVSLPPWIAGHPLGQ-VLRKALNKDPRQRAASAP 238

                   ..
gi 26051218    266 AL 267
Cdd:TIGR03903  239 AL 240
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
69-267 1.13e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 108.95  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   69 KHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAR--EY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL 144
Cdd:PTZ00267 123 DHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRlkEHlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  145 ASKckgAAVKLADFGLAIEVQGDQQAWFG--FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL 222
Cdd:PTZ00267 203 MPT---GIIKLGDFGFSKQYSDSVSLDVAssFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREI 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 26051218  223 YQQIKAGAYD-FPSPewdtVTPEAKNLINQMLTINPAKRITAHEAL 267
Cdd:PTZ00267 280 MQQVLYGKYDpFPCP----VSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
14-271 1.14e-25

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: 105.93  E-value: 1.14e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsardhqKLE----------REARICRLLKHSNIVRLHDSISEE 83
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI-----------RLEheegapftaiREASLLKDLKHANIVTLHDIIHTK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 G-----FHYLVFDLVT-----GGELFEDIVAREYYseadashciqQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAV 153
Cdd:cd07844  71 KtltlvFEYLDTDLKQymddcGGGLSMHNVRLFLF----------QLLRGLAYCHQRRVLHRDLKPQNLLISER---GEL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 154 KLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPF----WDEDQ-HKLYQ--- 224
Cdd:cd07844 138 KLADFGLARAKSVPSKTYSNEVVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQlHKIFRvlg 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 225 --------------QIKAGAYDFPSPE-----WDTV--TPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07844 218 tpteetwpgvssnpEFKPYSFPFYPPRplinhAPRLdrIPHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
14-271 1.34e-25

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: 105.52  E-value: 1.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE-REARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05605   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGEL-----------FEDIVAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA 161
Cdd:cd05605  82 MNGGDLkfhiynmgnpgFEEERAVFYAAE---------ITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTV 241
Cdd:cd05605 150 VEIP-EGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKF 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 242 TPEAKNLINQMLTINPAKRI-----TAHEALKHPW 271
Cdd:cd05605 229 SEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPF 263
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
12-271 3.94e-25

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: 105.39  E-value: 3.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHY 87
Cdd:cd05619   5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKAL--KKdvvLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIE-VQG 166
Cdd:cd05619  83 FVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLD---KDGHIKIADFGMCKEnMLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAgayDFP-SPEWdtVTPEA 245
Cdd:cd05619 160 DAKT-STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRM---DNPfYPRW--LEKEA 233
                       250       260
                ....*....|....*....|....*..
gi 26051218 246 KNLINQMLTINPAKRITAHEALK-HPW 271
Cdd:cd05619 234 KDILVKLFVREPERRLGVRGDIRqHPF 260
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
12-253 4.01e-25

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: 106.64  E-value: 4.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRrCVKLCTGHE-YAAKIINTKKLSARDHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLV 89
Cdd:cd05623  72 EDFEILKVIGRGAFGEVA-VVKLKNADKvFAMKILNKWEMLKRAETACFREERDVLVNGDSQwITTLHYAFQDDNNLYLV 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGEL------FEDIVAREYyseadASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE 163
Cdd:cd05623 151 MDYYVGGDLltllskFEDRLPEDM-----ARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMN---GHIRLADFGSCLK 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAWFGFA-GTPGYLSPEVLR-----KEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI--KAGAYDFPS 235
Cdd:cd05623 223 LMEDGTVQSSVAvGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKERFQFPT 302
                       250
                ....*....|....*...
gi 26051218 236 PEWDtVTPEAKNLINQML 253
Cdd:cd05623 303 QVTD-VSENAKDLIRRLI 319
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
13-271 5.78e-25

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: 105.88  E-value: 5.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREarICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd05600  12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNevnHVLTERD--ILTTTNSPWLVKLLYAFQDPENVYLA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA-------- 161
Cdd:cd05600  90 MEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSS---GHIKLTDFGLAsgtlspkk 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEV-----------------------------QGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYP 212
Cdd:cd05600 167 IESmkirleevkntafleltakerrniyramrKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFP 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 213 PFW----DEDQHKLY---QQIKAGAYDFPSPEWDtVTPEAKNLINQMLTiNPAKRITAHEALK-HPW 271
Cdd:cd05600 247 PFSgstpNETWANLYhwkKTLQRPVYTDPDLEFN-LSDEAWDLITKLIT-DPQDRLQSPEQIKnHPF 311
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-274 5.95e-25

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: 103.59  E-value: 5.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd06645  89 FCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN---GHVKLADFGVSAQITATIAKR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFWdeDQHKLYQQIKAGAYDFPSPEW-DTV--TPEA 245
Cdd:cd06645 166 KSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMTKSNFQPPKLkDKMkwSNSF 243
                       250       260
                ....*....|....*....|....*....
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd06645 244 HHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
12-272 6.76e-25

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: 103.57  E-value: 6.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06643   5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK--SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ 168
Cdd:cd06643  83 FCAGGAV--DAVMLELerpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD---GDIKLADFGVSAKNTRTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFAGTPGYLSPEVLRKEA-----YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI-KAGAYDFPSP-EWdtv 241
Cdd:cd06643 158 QRRDSFIGTPYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIaKSEPPTLAQPsRW--- 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06643 235 SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
9-214 8.02e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 107.19  E-value: 8.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    9 RFTDEYQLYEDIGKGAFSVVRR--CVKLctGHEYAAKIIntkKLS-ARDHQ---KLEREARICRLLKHSNIVRLHDSISE 82
Cdd:NF033483   4 LLGGRYEIGERIGRGGMAEVYLakDTRL--DRDVAVKVL---RPDlARDPEfvaRFRREAQSAASLSHPNIVSVYDVGED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   83 EGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI 162
Cdd:NF033483  79 GGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIAR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218  163 evqgdqqawfgfA-------------GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:NF033483 156 ------------AlssttmtqtnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
13-261 9.09e-25

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: 103.97  E-value: 9.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN----IVRLHDSISEEGFHYL 88
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcpfIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQgdQ 168
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEF---GHVRISDLGLACDFS--K 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFAGTPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVGYPPFWD---EDQHKLYQQIKAGAYDFPspewDTVTPE 244
Cdd:cd14223 156 KKPHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTMAVELP----DSFSPE 231
                       250
                ....*....|....*..
gi 26051218 245 AKNLINQMLTINPAKRI 261
Cdd:cd14223 232 LRSLLEGLLQRDVNRRL 248
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
12-281 9.42e-25

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: 103.19  E-value: 9.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklsarDHQKLER---EARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd06644  12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK-----SEEELEDymvEIEILATCNHPYIVKLLGAFYWDGKLWI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ 165
Cdd:cd06644  87 MIEFCPGGAV--DAIMLELdrgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD---GDIKLADFGVSAKNV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAWFGFAGTPGYLSPEV-----LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQI-KAGAYDFPSP-EW 238
Cdd:cd06644 162 KTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIaKSEPPTLSQPsKW 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 26051218 239 dtvTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASM 281
Cdd:cd06644 242 ---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPL 281
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
20-271 1.13e-24

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: 103.49  E-value: 1.13e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKK---LSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKAL--KKdvvLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIE-VQGDQQAwFGF 174
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLD---RDGHIKIADFGMCKEnVFGDNRA-STF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAgayDFPS-PEWdtVTPEAKNLINQML 253
Cdd:cd05620 157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV---DTPHyPRW--ITKESKDILEKLF 231
                       250
                ....*....|....*....
gi 26051218 254 TINPAKRITAHEALK-HPW 271
Cdd:cd05620 232 ERDPTRRLGVVGNIRgHPF 250
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
14-270 1.34e-24

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: 102.76  E-value: 1.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE-REARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQgDQQA 170
Cdd:cd05631  82 MNGGDLKFHIynMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDR---GHIRISDLGLAVQIP-EGET 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF--------WDEdqhkLYQQIKAGAYDFPspewDTVT 242
Cdd:cd05631 158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrkervkREE----VDRRVKEDQEEYS----EKFS 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 243 PEAKNLINQMLTINPAKRI-----TAHEALKHP 270
Cdd:cd05631 230 EDAKSICRMLLTKNPKERLgcrgnGAAGVKQHP 262
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
14-270 1.45e-24

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: 102.50  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCV-KLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLK---HSNIVRLHDSISEEGFHYLV 89
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA----- 161
Cdd:cd14052  82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFE---GTLKIGDFGMAtvwpl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 ---IEVQGDQQawfgfagtpgYLSPEVLRKEAYGKPVDIWACGVILY--ILLVGYPpfwDEDQHklYQQIKAGAY-DFP- 234
Cdd:cd14052 159 irgIEREGDRE----------YIAPEILSEHMYDKPADIFSLGLILLeaAANVVLP---DNGDA--WQKLRSGDLsDAPr 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 235 ---------------SPEWDTVTPEAKN----LINQMLTINPAKRITAHEALKHP 270
Cdd:cd14052 224 lsstdlhsasspssnPPPDPPNMPILSGsldrVVRWMLSPEPDRRPTADDVLATP 278
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
20-214 1.79e-24

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: 102.95  E-value: 1.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINT-KKLSARDHQKleREARICRLLKHSNIVRLHdSISEE--GFH-YLVFDLVTG 95
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDVQM--REFEVLKKLNHKNIVKLF-AIEEEltTRHkVLVMELCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELF---EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAV-KLADFGLAIEVQGDQQaW 171
Cdd:cd13988  78 GSLYtvlEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARELEDDEQ-F 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26051218 172 FGFAGTPGYLSPE-----VLRKEA---YGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd13988 157 VSLYGTEEYLHPDmyeraVLRKDHqkkYGATVDLWSIGVTFYHAATGSLPF 207
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
12-264 1.92e-24

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: 103.60  E-value: 1.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSN----IVRLHDSISEEGFHY 87
Cdd:cd05633   5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcpfIVCMTYAFHTPDKLC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQgd 167
Cdd:cd05633  85 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHVRISDLGLACDFS-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRK-EAYGKPVDIWACGVILYILLVGYPPFWD---EDQHKLYQQIKAGAYDFPspewDTVTP 243
Cdd:cd05633 160 KKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELP----DSFSP 235
                       250       260
                ....*....|....*....|.
gi 26051218 244 EAKNLINQMLTINPAKRITAH 264
Cdd:cd05633 236 ELKSLLEGLLQRDVSKRLGCH 256
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
20-272 1.93e-24

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: 102.03  E-value: 1.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIN---TKKLSARDHQKLEREARICRLLKHSNIVRLHDSIS--EEGFHYLVFDLVT 94
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIFVEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd06653  90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDS---AGNVKLGDFGASKRIQTICMSGTGI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 ---AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPfWDEdqHKLYQQIKAGAYDFPSPEW-DTVTPEAKNLIN 250
Cdd:cd06653 167 ksvTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPP-WAE--YEAMAAIFKIATQPTKPQLpDGVSDACRDFLR 243
                       250       260
                ....*....|....*....|..
gi 26051218 251 QMLtINPAKRITAHEALKHPWV 272
Cdd:cd06653 244 QIF-VEEKRRPTAEFLLRHPFV 264
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
20-274 2.71e-24

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: 101.27  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQIL-RELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 edivaREYYSEADA--SHCIQQILEAVLHC-----HQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAwf 172
Cdd:cd06605  87 -----DKILKEVGRipERILGKIAVAVVKGliylhEKHKIIHRDVKPSNILVNSR---GQVKLCDFGVSGQLVDSLAK-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVG---YPPFWDEDQHKLYQQIKAgAYDFPSPEW--DTVTPEAKN 247
Cdd:cd06605 157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrfpYPPPNAKPSMMIFELLSY-IVDEPPPLLpsGKFSPDFQD 235
                       250       260
                ....*....|....*....|....*..
gi 26051218 248 LINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd06605 236 FVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
11-272 3.08e-24

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: 101.61  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQK-LEREARICRLL-KHSNIVRLH------DSISE 82
Cdd:cd06608   5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIE----DEEEeIKLEINILRKFsNHPNIATFYgafikkDPPGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADF 158
Cdd:cd06608  81 DDQLWLVMEYCGGGsvtDLVKGLRKKgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EEAEVKLVDF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLAIEVQGDQQAWFGFAGTPGYLSPEVL-----RKEAYGKPVDIWACGVILYILLVGYPPFwdEDQH---KLYQQIKAGA 230
Cdd:cd06608 158 GVSAQLDSTLGRRNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIELADGKPPL--CDMHpmrALFKIPRNPP 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 26051218 231 YDFPSPE-WdtvTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06608 236 PTLKSPEkW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-260 5.12e-24

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: 100.87  E-value: 5.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINT-KKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIV----AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGD 167
Cdd:cd08228  83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITAT---GVVKLGDLGLGRFFSSK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKN 247
Cdd:cd08228 160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPTEHYSEKLRE 239
                       250
                ....*....|...
gi 26051218 248 LINQMLTINPAKR 260
Cdd:cd08228 240 LVSMCIYPDPDQR 252
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
20-269 6.80e-24

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: 100.31  E-value: 6.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCV---KLCTGHEYAAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd00192   3 LGEGAFGEVYKGKlkgGDGKTVDVAVKTLK-EDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 EL---------FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGD 167
Cdd:cd00192  82 DLldflrksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGED---LVVKISDFGLSRDIYDD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QqawFGFAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEWdtV 241
Cdd:cd00192 159 D---YYRKKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKG-YRLPKPEN--C 232
                       250       260
                ....*....|....*....|....*...
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKH 269
Cdd:cd00192 233 PDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
12-271 6.99e-24

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: 100.85  E-value: 6.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd07871   5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 lvtggelFEDIVAREYYSEADASHCIQ-------QILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV 164
Cdd:cd07871  84 -------YLDSDLKQYLDNCGNLMSMHnvkifmfQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLARAK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQI------------- 226
Cdd:cd07871 154 SVPTKTYSNEVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFpgstVKEELHLIFRLLgtpteetwpgvts 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 227 --KAGAYDFP----------SPEWDTvtpEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07871 234 neEFRSYLFPqyraqplinhAPRLDT---DGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
20-264 7.01e-24

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: 102.40  E-value: 7.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREarICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05626   9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNqvaHVKAERD--ILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGL---------------- 160
Cdd:cd05626  87 DMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLD---GHIKLTDFGLctgfrwthnskyyqkg 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 ---------------------------AIEVQGDQQAWFGFA----GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLV 209
Cdd:cd05626 164 shirqdsmepsdlwddvsncrcgdrlkTLEQRATKQHQRCLAhslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 210 GYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQM-------LTINPAKRITAH 264
Cdd:cd05626 244 GQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLccsaeerLGRNGADDIKAH 305
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
10-272 7.05e-24

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: 101.29  E-value: 7.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLcTGHEYAAKIINTKKLSARD------HQKLEREARICRLLKHSNIVRLHDSISEE 83
Cdd:cd14041   4 LNDRYLLLHLLGRGGFSEVYKAFDL-TEQRYVAVKIHQLNKNWRDekkenyHKHACREYRIHKELDHPRIVKLYDYFSLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHY-LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKCKGAAVKLADFGL 160
Cdd:cd14041  83 TDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITDFGL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AI--------EVQGDQQAWFGfAGTPGYLSPE--VLRKE--AYGKPVDIWACGVILYILLVGYPPF-WDEDQHKLYQQ-- 225
Cdd:cd14041 163 SKimdddsynSVDGMELTSQG-AGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQEnt 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 226 -IKAGAYDFPSPEwdTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14041 242 iLKATEVQFPPKP--VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
10-271 8.08e-24

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: 100.91  E-value: 8.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYED---IGKGAFSVVRRCVKLCTGHEYAAKII---NTKK---LSARdhqkleREARICRLLKHSNIVRLHDSI 80
Cdd:cd07865   7 FCDEVSKYEKlakIGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEgfpITAL------REIKILQLLKHENVVNLIEIC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEE--------GFHYLVFDLVT---GGELFEDIVAreyYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcK 149
Cdd:cd07865  81 RTKatpynrykGSIYLVFEFCEhdlAGLLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILIT---K 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 150 GAAVKLADFGLA----IEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVI--------------------- 203
Cdd:cd07865 155 DGVLKLADFGLArafsLAKNSQPNRYTNRVVTLWYRPPELLLGERdYGPPIDMWGAGCImaemwtrspimqgnteqhqlt 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 204 LYILLVGY--PPFW-DEDQHKLYQQIKagaydFPSPEWDTVT---------PEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07865 235 LISQLCGSitPEVWpGVDKLELFKKME-----LPQGQKRKVKerlkpyvkdPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
14-271 8.23e-24

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: 100.59  E-value: 8.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGheyaaKIINTKKLSARDHQK-----LEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETH-----EIVALKRVRLDDDDEgvpssALREICLLKELKHKNIVRLYDVLHSDKKLTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDlvtggelFEDIVAREYYS----EADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLA 161
Cdd:cd07839  77 VFE-------YCDQDLKKYFDscngDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLLIN---KNGELKLADFGLA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFGFAGTPGYLSPEVL-RKEAYGKPVDIWACGVILYILLVGYPPFWD----EDQHKLYQQI---------- 226
Cdd:cd07839 147 RAFGIPVRCYSAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQLKRIFRLlgtpteeswp 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 227 ---KAGAYDF-----PSPEWDTVTP----EAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07839 227 gvsKLPDYKPypmypATTSLVNVVPklnsTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
14-272 9.50e-24

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: 99.66  E-value: 9.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSarDHQKLEREARI---CRLLKH-----SNIVRLHDSISEEGF 85
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVS--EWGELPNGTRVpmeIVLLKKvgsgfRGVIRLLDWFERPDS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTG-GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAIEV 164
Cdd:cd14100  80 FVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI--DLNTGELKLIDFGSGALL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QgdQQAWFGFAGTPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFwDEDqhklyQQIKAGAYDFPSpewdTVTP 243
Cdd:cd14100 158 K--DTVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF-EHD-----EEIIRGQVFFRQ----RVSS 225
                       250       260
                ....*....|....*....|....*....
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14100 226 ECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
20-265 1.08e-23

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: 100.84  E-value: 1.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDH-QKLEREARICRLL---KHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEvESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVCFVMEYAAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVArEYYSEADA---SHCIQQILEavlHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd05589  87 GDLMMHIHE-DVFSEPRAvfyAACVVLGLQ---FLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCKEGMGFGDRTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGayDFPSPEWdtVTPEAKNLINQM 252
Cdd:cd05589 160 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVND--EVRYPRF--LSTEAISIMRRL 235
                       250
                ....*....|...
gi 26051218 253 LTINPAKRITAHE 265
Cdd:cd05589 236 LRKNPERRLGASE 248
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
48-271 1.43e-23

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: 101.01  E-value: 1.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  48 KKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGfHYLVFDLVTGGELFEDIVAREYYsEADASHCIQ------ 118
Cdd:cd07854  36 KKIVLTDPQSVKhalREIKIIRRLDHDNIVKVYEVLGPSG-SDLTEDVGSLTELNSVYIVQEYM-ETDLANVLEqgplse 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 119 --------QILEAVLHCHQMGVVHRDLKPENLLLASkcKGAAVKLADFGLAIEVQGDqqawFGFAG-------TPGYLSP 183
Cdd:cd07854 114 eharlfmyQLLRGLKYIHSANVLHRDLKPANVFINT--EDLVLKIGDFGLARIVDPH----YSHKGylseglvTKWYRSP 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 184 E-VLRKEAYGKPVDIWACGVILYILLVGYPPF-------------------WDEDQHKLYQQIkagAYDFPSPEWD---- 239
Cdd:cd07854 188 RlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpvvREEDRNELLNVI---PSFVRNDGGEprrp 264
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26051218 240 ------TVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07854 265 lrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPY 302
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
13-272 1.45e-23

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: 99.33  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEP--GDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd06646  88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADFGVAAKITATIAKRK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKE---AYGKPVDIWACGVILYILLVGYPPFWdeDQHKLYQQIKAGAYDFPSPEWDTVT---PEAK 246
Cdd:cd06646 165 SFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMF--DLHPMRALFLMSKSNFQPPKLKDKTkwsSTFH 242
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06646 243 NFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
14-272 3.71e-23

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: 99.80  E-value: 3.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAakiinTKKLSaRDHQKLE------REARICRLLKHSNIVRLHDSI----SEE 83
Cdd:cd07850   2 YQNLKPIGSGAQGIVCAAYDTVTGQNVA-----IKKLS-RPFQNVThakrayRELVLMKLVNHKNIIGLLNVFtpqkSLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFH--YLVFDLVTGGelFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLA 161
Cdd:cd07850  76 EFQdvYLVMELMDAN--LCQVIQMDLDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 ievqgdQQAWFGFAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILYILLVG---YPPFWDEDQ-HKLYQQI------ 226
Cdd:cd07850 150 ------RTAGTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIRGtvlFPGTDHIDQwNKIIEQLgtpsde 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 227 -----------------KAGAYDF-----------PSPEWDTVTPE-AKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07850 224 fmsrlqptvrnyvenrpKYAGYSFeelfpdvlfppDSEEHNKLKASqARDLLSKMLVIDPEKRISVDDALQHPYI 298
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
97-272 4.64e-23

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: 97.72  E-value: 4.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVKLADFGLAIEVQgdQQAWFGFAG 176
Cdd:cd14102  91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV--DLRTGELKLIDFGSGALLK--DTVYTDFDG 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAY-GKPVDIWACGVILYILLVGYPPFwDEDqhklyQQIKAGAYDFPSpewdTVTPEAKNLINQMLTI 255
Cdd:cd14102 167 TRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPF-EQD-----EEILRGRLYFRR----RVSPECQQLIKWCLSL 236
                       170
                ....*....|....*..
gi 26051218 256 NPAKRITAHEALKHPWV 272
Cdd:cd14102 237 RPSDRPTLEQIFDHPWM 253
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
20-271 5.38e-23

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: 99.21  E-value: 5.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHD----SISEEGFH--YLVFDLv 93
Cdd:cd07879  23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDvftsAVSGDEFQdfYLVMPY- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 tggeLFEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQaw 171
Cdd:cd07879 102 ----MQTDLqkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCE---LKILDFGLARHADAEMT-- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ-HKLYQQIKAGAYdfPSPE------------ 237
Cdd:cd07879 173 -GYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYlDQLTQILKVTGV--PGPEfvqkledkaaks 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 238 ----------------WDTVTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07879 250 yikslpkyprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
14-260 6.80e-23

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: 98.18  E-value: 6.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-SARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd08229  26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ 168
Cdd:cd08229 106 ADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITAT---GVVKLGDLGLGRFFSSKT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDeDQHKLYQQIKA-GAYDFPSPEWDTVTPEAKN 247
Cdd:cd08229 183 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLYSLCKKiEQCDYPPLPSDHYSEELRQ 261
                       250
                ....*....|...
gi 26051218 248 LINQMLTINPAKR 260
Cdd:cd08229 262 LVNMCINPDPEKR 274
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
13-352 7.24e-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: 99.34  E-value: 7.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSA-RDHQKLEREARIC-RLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05618  21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDdEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQA 170
Cdd:cd05618 101 EYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE---GHIKLTDYGMCKEGLRPGDT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF------WDEDQHK---LYQQIKAGAYDFPSpewdTV 241
Cdd:cd05618 178 TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssDNPDQNTedyLFQVILEKQIRIPR----SL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 242 TPEAKNLINQMLTINPAKRITAH------EALKHPWVcqRSTVASMMHRQETVECLKKfnarrKLKGAILTTMLATRnFS 315
Cdd:cd05618 254 SVKAASVLKSFLNKDPKERLGCHpqtgfaDIQGHPFF--RNVDWDLMEQKQVVPPFKP-----NISGEFGLDNFDSQ-FT 325
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 26051218 316 ARKQEIIKTTEQLIEAVNNGDFEAYAKIcDPGLTSFE 352
Cdd:cd05618 326 NEPVQLTPDDDDIVRKIDQSEFEGFEYI-NPLLMSAE 361
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-263 7.27e-23

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: 97.96  E-value: 7.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   8 TRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEgFHY 87
Cdd:cd14049   2 SRYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEH-VQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGE--LFEDIVAR-----EYYSEADASHCI---------QQILEAVLHCHQMGVVHRDLKPENLLL-ASKCKg 150
Cdd:cd14049  81 MLYIQMQLCElsLWDWIVERnkrpcEEEFKSAPYTPVdvdvttkilQQLLEGVTYIHSMGIVHRDLKPRNIFLhGSDIH- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 151 aaVKLADFGLAIEVQ-GDQQAWF-----------GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVgypPFWDE- 217
Cdd:cd14049 160 --VRIGDFGLACPDIlQDGNDSTtmsrlnglthtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEm 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 26051218 218 DQHKLYQQIKAGayDFPSpEWDTVTPEAKNLINQMLTINPAKRITA 263
Cdd:cd14049 235 ERAEVLTQLRNG--QIPK-SLCKRWPVQAKYIKLLTSTEPSERPSA 277
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
14-272 7.65e-23

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: 99.33  E-value: 7.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQDVY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAievqgdQQA 170
Cdd:cd07876 103 LVMELMDANLCQVIHMELDherMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLA------RTA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTP-----GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ----HKLYQQIKAGAYDFPS------ 235
Cdd:cd07876 174 CTNFMMTPyvvtrYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHidqwNKVIEQLGTPSAEFMNrlqptv 253
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 236 -------------------PEW--------DTV-TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07876 254 rnyvenrpqypgisfeelfPDWifpseserDKLkTSQARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
12-271 8.33e-23

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: 98.15  E-value: 8.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVrrcvklctgheYAAKIINTKKLSARDHQKLE----------REARICRLLKHSNIVRLHDSIS 81
Cdd:cd07873   2 ETYIKLDKLGEGTYATV-----------YKGRSKLTDNLVALKEIRLEheegapctaiREVSLLKDLKHANIVTLHDIIH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 EEGFHYLVFDlvtggelFEDIVAREYYSEADAS---HCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVK 154
Cdd:cd07873  71 TEKSLTLVFE-------YLDKDLKQYLDDCGNSinmHNVKlflfQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 155 LADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQI--- 226
Cdd:cd07873 141 LADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFpgstVEEQLHFIFRILgtp 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 227 ------------KAGAYDFPSPEWDTV---TPEAKN----LINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07873 221 teetwpgilsneEFKSYNYPKYRADALhnhAPRLDSdgadLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
18-282 9.22e-23

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: 97.43  E-value: 9.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd06640  10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd06640  88 SAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIKRNTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPfwDEDQHKLYQQIKAGAYDFPSPEWDtVTPEAKNLINQMLTIN 256
Cdd:cd06640 164 TPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP--NSDMHPMRVLFLIPKNNPPTLVGD-FSKPFKEFIDACLNKD 240
                       250       260
                ....*....|....*....|....*.
gi 26051218 257 PAKRITAHEALKHPWVCQRSTVASMM 282
Cdd:cd06640 241 PSFRPTAKELLKHKFIVKNAKKTSYL 266
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
20-214 1.30e-22

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: 96.96  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVkLCTGHEYAAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14066   1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMN-CAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIvareyyseadasHC---------------IQQILEAVLHCHQMG---VVHRDLKPENLLLAskcKGAAVKLADFGLA 161
Cdd:cd14066  79 DRL------------HChkgspplpwpqrlkiAKGIARGLEYLHEECpppIIHGDIKSSNILLD---EDFEPKLTDFGLA 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 162 --IEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14066 144 rlIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV 198
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
20-271 1.68e-22

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: 96.69  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS---ARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLV--FDLVT 94
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd06651  95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS---AGNVKLGDFGASKRLQTICMSGTGI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 ---AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEwdTVTPEAKNLINQ 251
Cdd:cd06651 172 rsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS--HISEHARDFLGC 249
                       250       260
                ....*....|....*....|
gi 26051218 252 MLtINPAKRITAHEALKHPW 271
Cdd:cd06651 250 IF-VEARHRPSAEELLRHPF 268
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
10-272 3.20e-22

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: 96.28  E-value: 3.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTgHEYAAKIINTKKLSARD------HQKLEREARICRLLKHSNIVRLHDSISEE 83
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVYKAFDLYE-QRYAAVKIHQLNKSWRDekkenyHKHACREYRIHKELDHPRIVKLYDYFSLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHY-LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKCKGAAVKLADFGL 160
Cdd:cd14040  83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AIEVQGDQQAWFGF------AGTPGYLSPE--VLRKE--AYGKPVDIWACGVILYILLVGYPPF-WDEDQHKLYQQ---I 226
Cdd:cd14040 163 SKIMDDDSYGVDGMdltsqgAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 26051218 227 KAGAYDFPSPEwdTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14040 243 KATEVQFPVKP--VVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
20-268 3.71e-22

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: 95.20  E-value: 3.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklctgheYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd14058   1 VGRGSFGVVCKAR-------WRNQIVAVKIIESESEKKaFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDIVAREYYSEADASHCIQ---QILEAVLHCHQMG---VVHRDLKPENLLLASkcKGAAVKLADFGLAIEVQG---DQQ 169
Cdd:cd14058  74 YNVLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTN--GGTVLKICDFGTACDISThmtNNK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 awfgfaGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFwDEDQHKLYQQIKAgAYDFPSPEWDTVTPEA-KNL 248
Cdd:cd14058 152 ------GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-DHIGGPAFRIMWA-VHNGERPPLIKNCPKPiESL 223
                       250       260
                ....*....|....*....|
gi 26051218 249 INQMLTINPAKRITAHEALK 268
Cdd:cd14058 224 MTRCWSKDPEKRPSMKEIVK 243
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
18-282 7.92e-22

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: 94.74  E-value: 7.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd06642  10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAG 176
Cdd:cd06642  88 SAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIKRNTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFwdEDQHKLYQQIKAGAYDFPSPEWDTVTPeAKNLINQMLTIN 256
Cdd:cd06642 164 TPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN--SDLHPMRVLFLIPKNSPPTLEGQHSKP-FKEFVEACLNKD 240
                       250       260
                ....*....|....*....|....*.
gi 26051218 257 PAKRITAHEALKHPWVCQRSTVASMM 282
Cdd:cd06642 241 PRFRPTAKELLKHKFITRYTKKTSFL 266
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
20-268 8.60e-22

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: 96.65  E-value: 8.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD---HQKLEREarICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05625   9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNqvaHVKAERD--ILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQ----------G 166
Cdd:cd05625  87 DMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILID---RDGHIKLTDFGLCTGFRwthdskyyqsG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQ---------QAW----------------------------FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLV 209
Cdd:cd05625 164 DHlrqdsmdfsNEWgdpencrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 210 GYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQM-------LTINPAKRITAHEALK 268
Cdd:cd05625 244 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLcrgpedrLGKNGADEIKAHPFFK 309
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
14-272 9.58e-22

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: 95.37  E-value: 9.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGH-EYAAKIINTKKLSardHQKLEREARICRLL--------KHsnIVRLHDSISEEG 84
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRARDLARGNqEVAIKIIRNNELM---HKAGLKELEILKKLndadpddkKH--CIRLLRHFEHKN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVT----------GGELFEDIVAREYYSeadashciQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVK 154
Cdd:cd14135  77 HLCLVFESLSmnlrevlkkyGKNVGLNIKAVRSYA--------QQLFLALKHLKKCNILHADIKPDNILVNEKKN--TLK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 155 LADFGLAIEVQGDQQawfgfagTPgYL------SPEVLRKEAYGKPVDIWACGVILYILLVG---YPPFWDEDQHKLY-- 223
Cdd:cd14135 147 LCDFGSASDIGENEI-------TP-YLvsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTGkilFPGKTNNHMLKLMmd 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 224 -------QQIKAGAY---------DFPSPEWDTVTPEA-----------------------------------KNLINQM 252
Cdd:cd14135 219 lkgkfpkKMLRKGQFkdqhfdenlNFIYREVDKVTKKEvrrvmsdikptkdlktlligkqrlpdedrkkllqlKDLLDKC 298
                       330       340
                ....*....|....*....|
gi 26051218 253 LTINPAKRITAHEALKHPWV 272
Cdd:cd14135 299 LMLDPEKRITPNEALQHPFI 318
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
12-267 1.01e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 98.27  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFH--YLV 89
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANQklYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218    90 FDLVTGGELFEDIVAREYYSEADASHCI----QQILEAVLHCHQMG-------VVHRDLKPENLLL-------------A 145
Cdd:PTZ00266   93 MEFCDAGDLSRNIQKCYKMFGKIEEHAIvditRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLstgirhigkitaqA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   146 SKCKGAAV-KLADFGLAIEVqGDQQAWFGFAGTPGYLSPEVLRKE--AYGKPVDIWACGVILYILLVGYPPFWDEDQ-HK 221
Cdd:PTZ00266  173 NNLNGRPIaKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKANNfSQ 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 26051218   222 LYQQIKAGaydfPSPEWDTVTPEAKNLINQMLTINPAKRITAHEAL 267
Cdd:PTZ00266  252 LISELKRG----PDLPIKGKSKELNILIKNLLNLSAKERPSALQCL 293
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
14-270 1.12e-21

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: 93.53  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD-HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDrKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGG-----ELFEDIvareyySEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQ-- 165
Cdd:cd14050  83 CDTSlqqycEETHSL------PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGDFGLVVELDke 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 --GDQQAwfgfaGTPGYLSPEVLRKEaYGKPVDIWACGVIL-----YILLVGYPPFWdedqhklyQQIKAGayDFPSPEW 238
Cdd:cd14050 154 diHDAQE-----GDPRYMAPELLQGS-FTKAADIFSLGITIlelacNLELPSGGDGW--------HQLRQG--YLPEEFT 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 239 DTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14050 218 AGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
20-227 1.15e-21

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: 94.06  E-value: 1.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADA--SHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA-----IEVQGDQQA 170
Cdd:cd13978  80 KSLLEREIQDVPWSlrFRIIHEIALGMnfLHNMDPPLLHHDLKPENILLDNHFH---VKISDFGLSklgmkSISANRRRG 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRkEAYGKPV---DIWACGVILYILLVGYPPFWDEDQHKLYQQIK 227
Cdd:cd13978 157 TENLGGTPIYMAPEAFD-DFNKKPTsksDVYSFAIVIWAVLTRKEPFENAINPLLIMQIV 215
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
14-217 1.91e-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: 93.18  E-value: 1.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLS---ARDHQKLEREARICRLLKHSNIVRLHDSI--SEEGFHYL 88
Cdd:cd06652   4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESpetSKEVNALECEIQLLKNLLHERIVQYYGCLrdPQERTLSI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ 168
Cdd:cd06652  84 FMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSV---GNVKLGDFGASKRLQTIC 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 169 QAWFGF---AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPfWDE 217
Cdd:cd06652 161 LSGTGMksvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPP-WAE 211
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
10-271 3.30e-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: 93.78  E-value: 3.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKII-NTKKLsaRDHQKLEreARICRLLKH------SNIVRLHDSISE 82
Cdd:cd14134  10 LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKY--REAAKIE--IDVLETLAEkdpngkSHCVQLRDWFDY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS-----------KC- 148
Cdd:cd14134  86 RGHMCIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkKRq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 149 ----KGAAVKLADFGLAI---EVQGDqqawfgFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF------- 214
Cdd:cd14134 165 irvpKSTDIKLIDFGSATfddEYHSS------IVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqthdnle 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 215 -----------------------------------WDEDQ------HKLYQQIKAGAYDFpSPEWdtvtPEAKNLINQML 253
Cdd:cd14134 239 hlammerilgplpkrmirrakkgakyfyfyhgrldWPEGSssgrsiKRVCKPLKRLMLLV-DPEH----RLLFDLIRKML 313
                       330
                ....*....|....*...
gi 26051218 254 TINPAKRITAHEALKHPW 271
Cdd:cd14134 314 EYDPSKRITAKEALKHPF 331
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
14-272 5.33e-21

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: 93.47  E-value: 5.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDHQKLeREARICRLLK-------HSNIVRLHDSISEEGFH 86
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKP--AYFRQAM-LEIAILTLLNtkydpedKHHIVRLLDHFMHHGHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgAAVKLADFGLAIEv 164
Cdd:cd14212  78 CIVFELL-GVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDS-PEIKLIDFGSACF- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 qgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL---------------YILLV------GYPPFWDEDQ---- 219
Cdd:cd14212 155 --ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAaelflglplfpgnseYNQLSriiemlGMPPDWMLEKgknt 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 220 HKLYQQIKAG----AYDFPSP---EWDTVTPEAKN--------------------------------------LINQMLT 254
Cdd:cd14212 233 NKFFKKVAKSggrsTYRLKTPeefEAENNCKLEPGkryfkyktlediimnypmkkskkeqidkemetrlafidFLKGLLE 312
                       330
                ....*....|....*...
gi 26051218 255 INPAKRITAHEALKHPWV 272
Cdd:cd14212 313 YDPKKRWTPDQALNHPFI 330
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
19-269 8.41e-21

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: 91.60  E-value: 8.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDS----ISEEGFHYLVFDLVT 94
Cdd:cd14033   8 EIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSwkstVRGHKCIILVTELMT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCkgAAVKLADFGLAIEvqgdQQAWF 172
Cdd:cd14033  88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLhfLHSRCPPILHRDLKCDNIFITGPT--GSVKIGDLGLATL----KRASF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFA--GTPGYLSPEvLRKEAYGKPVDIWACGV-ILYILLVGYPPFWDEDQHKLYQQIKAGAYdfPSPEWDTVTPEAKNLI 249
Cdd:cd14033 162 AKSviGTPEFMAPE-MYEEKYDEAVDVYAFGMcILEMATSEYPYSECQNAAQIYRKVTSGIK--PDSFYKVKVPELKEII 238
                       250       260
                ....*....|....*....|
gi 26051218 250 NQMLTINPAKRITAHEALKH 269
Cdd:cd14033 239 EGCIRTDKDERFTIQDLLEH 258
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
9-270 1.02e-20

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: 92.77  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlSARDHQKLEreARICRLLKH------SNIVRLHDSISE 82
Cdd:cd14226  10 KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKK-AFLNQAQIE--VRLLELMNKhdtenkYYIVRLKRHFMF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLVTGgELFEDI-----------VAREYyseadashcIQQILEAVLHCHQ--MGVVHRDLKPENLLLASKcK 149
Cdd:cd14226  87 RNHLCLVFELLSY-NLYDLLrntnfrgvslnLTRKF---------AQQLCTALLFLSTpeLSIIHCDLKPENILLCNP-K 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 150 GAAVKLADFGLAIEVqGDQ-----QAWFgfagtpgYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQ-- 219
Cdd:cd14226 156 RSAIKIIDFGSSCQL-GQRiyqyiQSRF-------YRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQmn 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 220 --------------------HKLYQQIKAGAY---------DFPSPE---------WDTVTP------EA---------- 245
Cdd:cd14226 228 kivevlgmppvhmldqapkaRKFFEKLPDGTYylkktkdgkKYKPPGsrklheilgVETGGPggrragEPghtvedylkf 307
                       330       340
                ....*....|....*....|....*
gi 26051218 246 KNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14226 308 KDLILRMLDYDPKTRITPAEALQHS 332
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
20-271 1.09e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.52  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   20 IGKGAFSVVRRCVKLCTGHEYA---AKIINTKKLSARDHQKLE---------REARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLVGmcgihfttlRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   88 LVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA------ 161
Cdd:PTZ00024  97 LVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK---GICKIADFGLArrygyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  162 ---IEVQGDQQAWFGFAGTPG-----YLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPF------------------ 214
Cdd:PTZ00024 173 pysDTLSKDETMQRREEMTSKvvtlwYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFpgeneidqlgrifellgt 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218  215 -----WDEDQH-KLYQQikagaYDFPSP-EWDTVTPEAK----NLINQMLTINPAKRITAHEALKHPW 271
Cdd:PTZ00024 253 pnednWPQAKKlPLYTE-----FTPRKPkDLKTIFPNASddaiDLLQSLLKLNPLERISAKEALKHEY 315
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
13-271 1.13e-20

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: 91.63  E-value: 1.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAkIINTKKLSARDHQKLE--REARICRLLK---HSNIVRLHDSIS-----E 82
Cdd:cd07862   2 QYECVAEIGEGAYGKVFKARDLKNGGRFVA-LKRVRVQTGEEGMPLStiREVAVLRHLEtfeHPNVVRLFDVCTvsrtdR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVF-----DLVTggelFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLAD 157
Cdd:cd07862  81 ETKLTLVFehvdqDLTT----YLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIKLAD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLAiEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW---DEDQ-HKLYQQIkagayDF 233
Cdd:cd07862 154 FGLA-RIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRgssDVDQlGKILDVI-----GL 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 234 PSPE-W--DTVTPE---------------------AKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07862 228 PGEEdWprDVALPRqafhsksaqpiekfvtdidelGKDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
14-282 1.15e-20

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: 91.29  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEE--AEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd06641  84 LGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEH---GEVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAgayDFPSPEWDTVTPEAKNLINQM 252
Cdd:cd06641 160 *FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPK---NNPPTLEGNYSKPLKEFVEAC 236
                       250       260       270
                ....*....|....*....|....*....|
gi 26051218 253 LTINPAKRITAHEALKHPWVCQRSTVASMM 282
Cdd:cd06641 237 LNKEPSFRPTAKELLKHKFILRNAKKTSYL 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
20-269 1.28e-20

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: 90.25  E-value: 1.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVV-RRCVKlctGHEYAAKIINTKKlsardhqklEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd14059   1 LGSGAQGAVfLGKFR---GEEVAVKKVRDEK---------ETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVqGDQQAWFGFAGTP 178
Cdd:cd14059  69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYN---DVLKISDFGTSKEL-SEKSTKMSFAGTV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 179 GYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewDTVTPEAKNLINQMLTINPA 258
Cdd:cd14059 145 AWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVP--STCPDGFKLLMKQCWNSKPR 222
                       250
                ....*....|.
gi 26051218 259 KRITAHEALKH 269
Cdd:cd14059 223 NRPSFRQILMH 233
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
14-272 2.24e-20

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: 92.07  E-value: 2.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISE----EGFH--Y 87
Cdd:cd07874  19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPqkslEEFQdvY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGelFEDIVAREYYSEAdASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAiEVQGD 167
Cdd:cd07874  99 LVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLA-RTAGT 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL------YILLVG--YPPFWD-----------EDQHKLYQQI-- 226
Cdd:cd07874 172 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGrdYIDQWNkvieqlgtpcpEFMKKLQPTVrn 251
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 227 ------KAGAYDFPSPEWDTVTP-----------EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07874 252 yvenrpKYAGLTFPKLFPDSLFPadsehnklkasQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
20-214 2.38e-20

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: 90.48  E-value: 2.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklCTGHEYAAKII--NTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14146   2 IGVGGFGKVYRAT--WKGQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVV---HRDLKPENLLLASKCK-----GAAVKLADFGL 160
Cdd:cd14146  80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEhddicNKTLKITDFGL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 161 AIEVQGDQQawFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14146 160 AREWHRTTK--MSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
13-214 2.49e-20

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: 92.01  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRrCVKLCTGHE-YAAKIIntKKLSARDHQKLEREARICRLLKHSN----IVRLHDSISEEGFHY 87
Cdd:cd05617  16 DFDLIRVIGRGSYAKVL-LVRLKKNDQiYAMKVV--KKELVHDDEDIDWVQTEKHVFEQASsnpfLVGLHSCFQTTSRLF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGD 167
Cdd:cd05617  93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD---GHIKLTDYGMCKEGLGP 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 168 QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd05617 170 GDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
12-271 2.53e-20

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: 91.21  E-value: 2.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd07872   6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 lvtggelFEDIVAREYYSEAD---ASHCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV 164
Cdd:cd07872  85 -------YLDKDLKQYMDDCGnimSMHNVKiflyQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPF----WDEDQHKLYQQIKAGA--------- 230
Cdd:cd07872 155 SVPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFpgstVEDELHLIFRLLGTPTeetwpgiss 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 231 ------YDFP----------SPEWDTvtpEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07872 235 ndefknYNFPkykpqplinhAPRLDT---EGIELLTKFLQYESKKRISAEEAMKHAY 288
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
14-272 4.22e-20

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: 90.92  E-value: 4.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHSNIVRLHDSISEEGFHY------ 87
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKK---RFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYfrnhlc 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVtGGELFEDIVAREY--YSEAdashCIQQILEAVLHCHQM----GVVHRDLKPENLLLASKCKgAAVKLADFGLA 161
Cdd:cd14225 122 ITFELL-GMNLYELIKKNNFqgFSLS----LIRRFAISLLQCLRLlyreRIIHCDLKPENILLRQRGQ-SSIKVIDFGSS 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEvqgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAgAYDFPSPE---- 237
Cdd:cd14225 196 CY---EHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIME-VLGLPPPElien 271
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 238 -------WDT------VT--------PEAKNL--------------INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14225 272 aqrrrlfFDSkgnprcITnskgkkrrPNSKDLasalktsdplfldfIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
11-272 4.53e-20

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: 90.05  E-value: 4.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtkKLSARDhQKLEREARICRLL-KHSNIVRLHDSISEE-----G 84
Cdd:cd06639  21 SDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD--PISDVD-EEIEAEYNILRSLpNHPNVVKFYGMFYKAdqyvgG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGL 160
Cdd:cd06639  98 QLWLVLELCNGGsvtELVKGLLKCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AIEVQGDQQAWFGFAGTPGYLSPEVLRKE-----AYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGaydfPS 235
Cdd:cd06639 175 SAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRN----PP 250
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 26051218 236 PEwdTVTPEA-----KNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06639 251 PT--LLNPEKwcrgfSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
20-265 5.14e-20

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: 89.49  E-value: 5.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdhqklerEARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAE-------ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAvkLADFGLAIEVQGD---QQAWFG--F 174
Cdd:cd13991  87 QLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF--LCDFGHAECLDPDglgKSLFTGdyI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGaydfPSPEWDtVTPEAKNL----IN 250
Cdd:cd13991 165 PGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANE----PPPLRE-IPPSCAPLtaqaIQ 239
                       250
                ....*....|....*
gi 26051218 251 QMLTINPAKRITAHE 265
Cdd:cd13991 240 AGLRKEPVHRASAAE 254
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
11-272 6.00e-20

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: 89.69  E-value: 6.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  11 TDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtkklSARD-HQKLEREARICRLLK-HSNIVRLH------DSISE 82
Cdd:cd06638  17 SDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILD----PIHDiDEEIEAEYNILKALSdHPNVVKFYgmyykkDVKNG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFhYLVFDLVTGG---ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADF 158
Cdd:cd06638  93 DQL-WLVLELCNGGsvtDLVKGFLKRgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTT---EGGVKLVDF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLAIEVQGDQQAWFGFAGTPGYLSPEVLRKE-----AYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYD 232
Cdd:cd06638 169 GVSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADlHPMRALFKIPRNPPPT 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26051218 233 FPSPE-WdtvTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06638 249 LHQPElW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
12-272 7.00e-20

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: 89.40  E-value: 7.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARdHQKLEREARICRLLKHSNIVRLHDSISEE--GFHYLV 89
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDV-QKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELfeDIVAREYYSEAD--ASHCIQQILEAVL----HCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE 163
Cdd:cd06621  80 MEYCEGGSL--DSIYKKVKKKGGriGEKVLGKIAESVLkglsYLHSRKIIHRDIKPSNILLTRK---GQVKLCDFGVSGE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLyQQIKAGAY--DFPSPE---- 237
Cdd:cd06621 155 LVNSLAG--TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPL-GPIELLSYivNMPNPElkde 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26051218 238 ------WdtvTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06621 232 pengikW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
14-271 7.33e-20

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 91.25  E-value: 7.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHY----LV 89
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV------LQDPQYKNRELLIMKNLNHINIIFLKDYYYTECFKKneknIF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   90 FDLVTggELFEDIVAR--EYYSEADASHCI-------QQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLADFGL 160
Cdd:PTZ00036 142 LNVVM--EFIPQTVHKymKHYARNNHALPLflvklysYQLCRALAYIHSKFICHRDLKPQNLLIDPNTH--TLKLCDFGS 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  161 AIEVQGDQQAwFGFAGTPGYLSPEV-LRKEAYGKPVDIWACGVILYILLVGYPPFW------------------DEDQHK 221
Cdd:PTZ00036 218 AKNLLAGQRS-VSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSgqssvdqlvriiqvlgtpTEDQLK 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218  222 L----YQQIKAGayDFPSPEWDTVTP-----EAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:PTZ00036 297 EmnpnYADIKFP--DVKPKDLKKVFPkgtpdDAINFISQFLKYEPLKRLNPIEALADPF 353
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
14-161 8.74e-20

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: 88.67  E-value: 8.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLsardHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVFDL 92
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSK----HPQLEYEAKVYKLLQGGPgIPRLYWFGQEGDYNVMVMDL 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218  93 VtgGELFEDIvaREYYSE----------ADashciqQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA 161
Cdd:cd14016  78 L--GPSLEDL--FNKCGRkfslktvlmlAD------QMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLA 146
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
19-274 1.06e-19

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: 88.62  E-value: 1.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDS----ISEEGFHYLVFDLVT 94
Cdd:cd14031  17 ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSwesvLKGKKCIVLVTELMT 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCkgAAVKLADFGLAIEVQGDQQAwf 172
Cdd:cd14031  97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLqfLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLMRTSFAK-- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTPGYLSPEvLRKEAYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYdfPSPEWDTVTPEAKNLINQ 251
Cdd:cd14031 173 SVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSGIK--PASFNKVTDPEVKEIIEG 249
                       250       260
                ....*....|....*....|...
gi 26051218 252 MLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd14031 250 CIRQNKSERLSIKDLLNHAFFAE 272
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
20-204 1.14e-19

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: 87.93  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklctgHEYAAKIINTKKLSARDHQK-LEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGEL 98
Cdd:cd14065   1 LGKGFFGEVYKVT-----HRETGKVMVMKELKRFDEQRsFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 fEDIVAR--EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEV------QGDQQA 170
Cdd:cd14065  76 -EELLKSmdEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMpdektkKPDRKK 154
                       170       180       190
                ....*....|....*....|....*....|....
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14065 155 RLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
20-214 2.63e-19

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: 87.71  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHD------SISEEGFHYLVFDLV 93
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCR-QELSPKNRERWCLEIQIMKRLNHPNVVAARDvpeglqKLAPNDLPLLAMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELfedivaREYYS---------EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEV 164
Cdd:cd14038  81 QGGDL------RKYLNqfenccglrEGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKEL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26051218 165 qgDQQAW-FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14038 155 --DQGSLcTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
20-214 2.99e-19

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: 87.06  E-value: 2.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcvKLCTGHEYAAKIINT--KKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14061   2 IGVGGFGKVYR--GIWRGEEVAVKAARQdpDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQqILEAVLHCHQ---MGVVHRDLKPENLLLASKCKGA-----AVKLADFGLAIEVQGDQQ 169
Cdd:cd14061  80 LNRVLAGRKIPPHVLVDWAIQ-IARGMNYLHNeapVPIIHRDLKSSNILILEAIENEdlenkTLKITDFGLAREWHKTTR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 26051218 170 awFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14061 159 --MSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
20-263 4.43e-19

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: 86.90  E-value: 4.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklCTGHEYAAKIINTKKLSAR---------DHQKLE----------REARICRLLKHSNIVRLHDSi 80
Cdd:cd14000   2 LGDGGFGSVYRAS--YKGEPVAVKIFNKHTSSNFanvpadtmlRHLRATdamknfrllrQELTVLSHLHHPSIVYLLGI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 seeGFH--YLVFDLVTGGELfeDIVAREY-YSEADASHCIQQ-----ILEAVLHCHQMGVVHRDLKPENLLLASKCKGAA 152
Cdd:cd14000  79 ---GIHplMLVLELAPLGSL--DHLLQQDsRSFASLGRTLQQrialqVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 153 V--KLADFGlaIEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd14000 154 IiiKIADYG--ISRQCCRMGAKGSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGG 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 230 AYDfPSPEWDTVT-PEAKNLINQMLTINPAKRITA 263
Cdd:cd14000 232 LRP-PLKQYECAPwPEVEVLMKKCWKENPQQRPTA 265
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
20-267 1.08e-18

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: 85.64  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKiintKKLSARDHQKLEREARIC---RLLKHSNIVRLHD--SISEE-----GFHYLV 89
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALK----RLLSNEEEKNKAIIQEINfmkKLSGHPNIVQFCSaaSIGKEesdqgQAEYLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFE-------------DIVAREYYseadashciqQILEAVLHCH--QMGVVHRDLKPENLLLASKckgAAVK 154
Cdd:cd14036  84 LTELCKGQLVDfvkkveapgpfspDTVLKIFY----------QTCRAVQHMHkqSPPIIHRDLKIENLLIGNQ---GQIK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 155 LADFGLA-IEVQGDQQAWFGFA-----------GTPGYLSPEVLrkEAY-----GKPVDIWACGVILYILLVGYPPFwdE 217
Cdd:cd14036 151 LCDFGSAtTEAHYPDYSWSAQKrslvedeitrnTTPMYRTPEMI--DLYsnypiGEKQDIWALGCILYLLCFRKHPF--E 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 218 DQHKLyqQIKAGAYDFPSPewDTVTPEAKNLINQMLTINPAKRITAHEAL 267
Cdd:cd14036 227 DGAKL--RIINAKYTIPPN--DTQYTVFHDLIRSTLKVNPEERLSITEIV 272
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
20-159 1.11e-18

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: 82.10  E-value: 1.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLLK--HSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDV--NNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGT 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218  98 LFeDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFG 159
Cdd:cd13968  79 LI-AYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS---EDGNVKLIDFG 136
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
20-282 1.34e-18

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: 85.41  E-value: 1.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVrrcvklctgheYAAKIINT------KKLSARDHQKLE---REARICRLLK-HSNIVRLHDS----ISEEGF 85
Cdd:cd14037  11 LAEGGFAHV-----------YLVKTSNGgnraalKRVYVNDEHDLNvckREIEIMKRLSgHKNIVGYIDSsanrSGNGVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 H-YLVFDLVTGGELFEDIVAR--EYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGL 160
Cdd:cd14037  80 EvLLLMEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVCEAVaaMHYLKPPLIHRDLKVENVLISDSGN---YKLCDFGS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AIEVQGDQQAWFGFA---------GTPGYLSPEVLrkEAY-GKPV----DIWACGVILYILLVGYPPFwdEDQHKLyqQI 226
Cdd:cd14037 157 ATTKILPPQTKQGVTyveedikkyTTLQYRAPEMI--DLYrGKPIteksDIWALGCLLYKLCFYTTPF--EESGQL--AI 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 227 KAGAYDFPSpeWDTVTPEAKNLINQMLTINPAKRitahealkhPWVCQRSTVASMM 282
Cdd:cd14037 231 LNGNFTFPD--NSRYSKRLHKLIRYMLEEDPEKR---------PNIYQVSYEAFEL 275
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
20-264 1.88e-18

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: 85.94  E-value: 1.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIIntKKLSARDHQKLErearICRLLKH-----SN---IVRLHDSISEEGFHYLVFD 91
Cdd:cd05588   3 IGRGSYAKVLMVELKKTKRIYAMKVI--KKELVNDDEDID----WVQTEKHvfetaSNhpfLVGLHSCFQTESRLFFVIE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd05588  77 FVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSE---GHIKLTDYGMCKEGLRPGDTT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF------WDEDQHK---LYQQIKAGAYDFPSpewdTVT 242
Cdd:cd05588 154 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssDNPDQNTedyLFQVILEKPIRIPR----SLS 229
                       250       260
                ....*....|....*....|..
gi 26051218 243 PEAKNLINQMLTINPAKRITAH 264
Cdd:cd05588 230 VKAASVLKGFLNKNPAERLGCH 251
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
13-214 4.00e-18

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: 83.94  E-value: 4.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVklCTGHEYAAKII--NTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14145   7 ELVLEEIIGIGGFGKVYRAI--WIGDEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVAREYYSEADASHCIQqILEAVLHCHQMGVV---HRDLKPENLLLASKCKGA-----AVKLADFGLAI 162
Cdd:cd14145  85 EFARGGPLNRVLSGKRIPPDILVNWAVQ-IARGMNYLHCEAIVpviHRDLKSSNILILEKVENGdlsnkILKITDFGLAR 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 163 EVQgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14145 164 EWH--RTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
13-214 4.52e-18

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: 83.93  E-value: 4.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRcvklctgHEYAAKIINTKklSARDH---------QKLEREARICRLLKHSNIVRLHDSISEE 83
Cdd:cd14147   4 ELRLEEVIGIGGFGKVYR-------GSWRGELVAVK--AARQDpdedisvtaESVRQEARLFAMLAHPNIIALKAVCLEE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQqILEAVLHCHQ---MGVVHRDLKPENLLLASKCKG-----AAVKL 155
Cdd:cd14147  75 PNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQ-IARGMHYLHCealVPVIHRDLKSNNILLLQPIENddmehKTLKI 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 156 ADFGLAIEVQGDQQawFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14147 154 TDFGLAREWHKTTQ--MSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
14-272 4.75e-18

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: 85.10  E-value: 4.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd07875  26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEAD---ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAiEVQGDQQA 170
Cdd:cd07875 106 IVMELMDANLCQVIQMELDherMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLA-RTAGTSFM 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 WFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ----HKLYQQI-------------------- 226
Cdd:cd07875 182 MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHidqwNKVIEQLgtpcpefmkklqptvrtyve 261
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 227 ---KAGAYDFPSPEWDTVTP-----------EAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd07875 262 nrpKYAGYSFEKLFPDVLFPadsehnklkasQARDLLSKMLVIDASKRISVDEALQHPYI 321
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
14-272 5.43e-18

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: 85.18  E-value: 5.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsaRDHQKLEREARICRLLKHS------NIVRLHDSISEEGFHY 87
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEK---RFHRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHIC 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGgELFEDI-----------VAREYyseadaSHCIQQILEAVlhcHQMGVVHRDLKPENLLLASKCKgAAVKLA 156
Cdd:cd14224 144 MTFELLSM-NLYELIkknkfqgfslqLVRKF------AHSILQCLDAL---HRNKIIHCDLKPENILLKQQGR-SGIKVI 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 157 DFGLAIEvqgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQ---------------HK 221
Cdd:cd14224 213 DFGSSCY---EHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEgdqlacmiellgmppQK 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 222 LYQQIKAGAYDFPS---PEWDTVT----------------------PEAKNLINQM---------------LTINPAKRI 261
Cdd:cd14224 290 LLETSKRAKNFISSkgyPRYCTVTtlpdgsvvlnggrsrrgkmrgpPGSKDWVTALkgcddplfldflkrcLEWDPAARM 369
                       330
                ....*....|.
gi 26051218 262 TAHEALKHPWV 272
Cdd:cd14224 370 TPSQALRHPWL 380
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
12-271 6.53e-18

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: 83.97  E-value: 6.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd07869   5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTG----------GELFEDIVAREYYseadashciqQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA 161
Cdd:cd07869  84 YVHTdlcqymdkhpGGLHPENVKLFLF----------QLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFGFAGTPGYLSPEVLRKEA-YGKPVDIWACGVILYILLVG---YPPFWD-EDQ-HKLY-------QQIKA 228
Cdd:cd07869 151 RAKSVPSHTYSNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGvaaFPGMKDiQDQlERIFlvlgtpnEDTWP 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 229 GAYDFP--SPE-------------WDTVT--PEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07869 231 GVHSLPhfKPErftlyspknlrqaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEY 290
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
17-269 9.78e-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: 9.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDIG-----KGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDhqkLEREARicrlLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd13995   4 YRNIGsdfipRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSD---VEIQAC----FRHENIAELYGALLWEETVHLFME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckgAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd13995  77 AGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS----TKAVLVDFGLSVQMTEDVYVP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWD---TVTPEAKNL 248
Cdd:cd13995 153 KDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLEDiaqDCSPAMREL 232
                       250       260
                ....*....|....*....|.
gi 26051218 249 INQMLTINPAKRITAHEALKH 269
Cdd:cd13995 233 LEAALERNPNHRSSAAELLKH 253
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
19-274 1.50e-17

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: 82.49  E-value: 1.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDS-ISEEGFHYLVFDLVTGGE 97
Cdd:cd06620  12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQIL-RELQILHECHSPYIVSFYGAfLNENNNIIICMEYMDCGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LfeDIVAREY--YSEADASHCIQQILEAVLHCH-QMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ---GDQqaw 171
Cdd:cd06620  91 L--DKILKKKgpFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSK---GQIKLCDFGVSGELInsiADT--- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fgFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDF-------PSP---EWDTV 241
Cdd:cd06620 163 --FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLlqrivnePPPrlpKDRIF 240
                       250       260       270
                ....*....|....*....|....*....|...
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd06620 241 PKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
61-270 1.68e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 83.39  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   61 EARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGgELFEDIVAREYYSEADASHCIQ-QILEAVLHCHQMGVVHRDLKP 139
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRSRPLPIDQALIIEkQILEGLRYLHAQRIIHRDVKT 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  140 ENLLLASKckgAAVKLADFGlAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLvGYPP--FWDE 217
Cdd:PHA03209 186 ENIFINDV---DQVCIGDLG-AAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML-AYPStiFEDP 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  218 DQH-------------KLYQQIKAGAYDFPSPEWDTVTPE--------------------------AKNLINQMLTINPA 258
Cdd:PHA03209 261 PSTpeeyvkschshllKIISTLKVHPEEFPRDPGSRLVRGfieyaslerqpytrypcfqrvnlpidGEFLVHKMLTFDAA 340
                        250
                 ....*....|..
gi 26051218  259 KRITAHEALKHP 270
Cdd:PHA03209 341 MRPSAEEILNYP 352
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
13-271 2.64e-17

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: 82.87  E-value: 2.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISE---EGFH--Y 87
Cdd:cd07853   1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPphiDPFEeiY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLA-IEVQG 166
Cdd:cd07853  81 VVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCV---LKICDFGLArVEEPD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFAGTPGYLSPEVLR-KEAYGKPVDIWACGVI---------------------LYILLVGYPPFwdEDQHKLYQ 224
Cdd:cd07853 157 ESKHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIfaellgrrilfqaqspiqqldLITDLLGTPSL--EAMRSACE 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 225 QIKAGAYDFPSPEWDT---------VTPEAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07853 235 GARAHILRGPHKPPSLpvlytlssqATHEAVHLLCRMLVFDPDKRISAADALAHPY 290
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
9-271 2.70e-17

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: 82.36  E-value: 2.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   9 RFTDEYQLYEDIGKGAFSVVRRCVKLCTGH-EYAAKII-NTKKLsaRDHQKLEreARICRLLKHSN------IVRLHDSI 80
Cdd:cd14214  10 WLQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIrNVGKY--REAARLE--INVLKKIKEKDkenkflCVLMSDWF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAS-----------K 147
Cdd:cd14214  86 NFHGHMCIAFELL-GKNTFEFLKENNFqpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNsefdtlyneskS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 C-----KGAAVKLADFGLAievQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDED---- 218
Cdd:cd14214 165 CeeksvKNTSIRVADFGSA---TFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHEnreh 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 219 ------------QHKLYQQIKAGAYDFPSPEWDTVTPEAK------------------------NLINQMLTINPAKRIT 262
Cdd:cd14214 242 lvmmekilgpipSHMIHRTRKQKYFYKGSLVWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRIT 321

                ....*....
gi 26051218 263 AHEALKHPW 271
Cdd:cd14214 322 LKEALLHPF 330
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
19-272 2.77e-17

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: 82.39  E-value: 2.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVrrcvkLCTGHEYAAKIINTKKLSARDHQKLER------EARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd06633  28 EIGHGSFGAV-----YFATNSHTNEVVAIKKMSYSGKQTNEKwqdiikEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGG--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQa 170
Cdd:cd06633 103 CLGSasDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIASPANS- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 171 wfgFAGTPGYLSPEV---LRKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIKAGAYDFPSPEWdtvTPEAK 246
Cdd:cd06633 177 ---FVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNaMSALYHIAQNDSPTLQSNEW---TDSFR 250
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06633 251 GFVDYCLQKIPQERPSSAELLRHDFV 276
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
20-245 5.89e-17

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: 80.42  E-value: 5.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcvKLCTGHEYAAKII--NTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd14148   2 IGVGGFGKVYK--GLWRGEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIVAREYYSEADASHCIQqILEAVLHCHQMGVV---HRDLKPENLLLASKCK-----GAAVKLADFGLAIEVQGDQQ 169
Cdd:cd14148  80 LNRALAGKKVPPHVLVNWAVQ-IARGMNYLHNEAIVpiiHRDLKSSNILILEPIEnddlsGKTLKITDFGLAREWHKTTK 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 170 awFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPewdTVTPEA 245
Cdd:cd14148 159 --MSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIP---STCPEP 229
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
20-214 6.30e-17

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: 80.96  E-value: 6.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklctgHEYAAKIINTKK----LSARDHQKlER---EARICRLLKHSNIVRLHD------SISEEGFH 86
Cdd:cd13989   1 LGSGGFGYVTLWK-----HQDTGEYVAIKKcrqeLSPSDKNR-ERwclEVQIMKKLNHPNVVSARDvppeleKLSPNDLP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAREYYS---EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaSKCKGAAV-KLADFGLAI 162
Cdd:cd13989  75 LLAMEYCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVL-QQGGGRVIyKLIDLGYAK 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26051218 163 EVqgDQQAW-FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd13989 154 EL--DQGSLcTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
19-274 9.98e-17

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: 79.74  E-value: 9.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHD--SISEEGFH--YLVFDLVT 94
Cdd:cd14032   8 ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDfwESCAKGKRciVLVTELMT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMG--VVHRDLKPENLLLASKCkgAAVKLADFGLAIEvqgdQQAWF 172
Cdd:cd14032  88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPT--GSVKIGDLGLATL----KRASF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFA--GTPGYLSPEvLRKEAYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYdfPSPEWDTVTPEAKNLI 249
Cdd:cd14032 162 AKSviGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTCGIK--PASFEKVTDPEIKEII 238
                       250       260
                ....*....|....*....|....*
gi 26051218 250 NQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd14032 239 GECICKNKEERYEIKDLLSHAFFAE 263
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-262 1.00e-16

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: 79.85  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  23 GAFSVVRRCVKLCTGHeYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDI 102
Cdd:cd14027   4 GGFGKVSLCFHRTQGL-VVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 103 VAREYYSEADAsHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI---------EVQGDQQAWFG 173
Cdd:cd14027  83 KKVSVPLSVKG-RIILEIIEGMAYLHGKGVIHKDLKPENILVD---NDFHIKIADLGLASfkmwskltkEEHNEQREVDG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 F----AGTPGYLSPEVLRkEAYGKPV---DIWACGVILYILLVGYPPFWD---EDQhkLYQQIKAGAydfpSPEWDTVTP 243
Cdd:cd14027 159 TakknAGTLYYMAPEHLN-DVNAKPTeksDVYSFAIVLWAIFANKEPYENainEDQ--IIMCIKSGN----RPDVDDITE 231
                       250       260
                ....*....|....*....|...
gi 26051218 244 ----EAKNLINQMLTINPAKRIT 262
Cdd:cd14027 232 ycprEIIDLMKLCWEANPEARPT 254
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
20-218 1.02e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 81.58  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKK---LSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGg 96
Cdd:PHA03212  89 IEKAGFSILETFTPGAEGFAFACIDNKTCEhvvIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA-IEVQGDQQAWFGFA 175
Cdd:PHA03212 168 DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHP---GDVCLGDFGAAcFPVDINANKYYGWA 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 26051218  176 GTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDED 218
Cdd:PHA03212 245 GTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKD 287
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
12-272 1.17e-16

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: 79.89  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQII-MELDILHKAVSPYIVDFYGAFFIEGAVYMCME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELfEDIVAREYYSEADASHCIQQILEAVLHC-----HQMGVVHRDLKPENLLLASKckgAAVKLADFGlaieVQG 166
Cdd:cd06622  80 YMDAGSL-DKLYAGGVATEGIPEDVLRRITYAVVKGlkflkEEHNIIHRDVKPTNVLVNGN---GQVKLCDFG----VSG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 167 DQQAWFGFA--GTPGYLSPEVLRKE------AYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEW 238
Cdd:cd06622 152 NLVASLAKTniGCQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLP 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 239 DTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06622 232 SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
43-270 2.06e-16

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: 78.56  E-value: 2.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  43 KIINTKKlsarDHQKLEREARICRLLKHSNIVRLHD-SISEEGFH-----YLVFDLVTGGELFEDIVAREYYSEADASHC 116
Cdd:cd14012  34 KTSNGKK----QIQLLEKELESLKKLRHPNLVSYLAfSIERRGRSdgwkvYLLTEYAPGGSLSELLDSVGSVPLDTARRW 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQ--GDQQAWFGFAGTPgYLSPEVLR-KEAYGK 193
Cdd:cd14012 110 TLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLdmCSRGSLDEFKQTY-WLPPELAQgSKSPTR 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 194 PVDIWACGVILYILLVGYPPFwdedqhklyqQIKAGAYDFPSPewDTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14012 189 KTDVWDLGLLFLQMLFGLDVL----------EKYTSPNPVLVS--LDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
8-270 2.18e-16

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: 78.91  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   8 TRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGfH 86
Cdd:cd14138   1 SRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDD-H 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELFEDIVAR-----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-------------- 147
Cdd:cd14138  80 MLIQNEYCNGGSLADAISEnyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTsipnaaseegdede 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 CKGAAV--KLADFGLAIEVQGDQQAwfgfAGTPGYLSPEVLrKEAYG--KPVDIWACGVILyILLVGYPPF-WDEDQhkl 222
Cdd:cd14138 160 WASNKVifKIGDLGHVTRVSSPQVE----EGDSRFLANEVL-QENYThlPKADIFALALTV-VCAAGAEPLpTNGDQ--- 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 223 YQQIKAGAydFPS-PEwdTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14138 231 WHEIRQGK--LPRiPQ--VLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
15-274 2.40e-16

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: 78.65  E-value: 2.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYED---IGKGAFSVV--RRCVKLCtgheyaaKIINTKKLSARDHQKLER------EARICRLLKHSNIVRLHDSISEE 83
Cdd:cd06607   1 KIFEDlreIGHGSFGAVyyARNKRTS-------EVVAIKKMSYSGKQSTEKwqdiikEVKFLRQLRHPNTIEYKGCYLRE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHYLVFDLVTGGElfEDI--VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLA 161
Cdd:cd06607  74 HTAWLVMEYCLGSA--SDIveVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEP---GTVKLADFGSA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQawfgFAGTPGYLSPEV---LRKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIKAGAYDFPSPE 237
Cdd:cd06607 149 SLVCPANS----FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNDSPTLSSGE 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 238 WdtvTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd06607 225 W---SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
20-204 2.44e-16

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: 78.29  E-value: 2.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIintKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRANML-REVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA--IEVQGDQQAWFGFAGT 177
Cdd:cd14155  77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAekIPDYSDGKEKLAVVGS 156
                       170       180
                ....*....|....*....|....*..
gi 26051218 178 PGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14155 157 PYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
5-272 2.55e-16

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: 80.13  E-value: 2.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   5 VTCTrFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKleREARICRLLKHS----NIVRLHDSI 80
Cdd:cd14227   9 VLCS-MTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI--EVSILARLSTESaddyNFVRAYECF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVTggELFEDIVAREYYSEADASH---CIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLA 156
Cdd:cd14227  86 QHKNHTCLVFEMLE--QNLYDFLKQNKFSPLPLKYirpILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyRVKVI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 157 DFGLAIEVQgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVG---YPPFWDEDQHKLYQQ-------- 225
Cdd:cd14227 164 DFGSASHVS--KAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGwplYPGASEYDQIRYISQtqglpaey 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 226 -IKAGA---------YDFPSPEWDTVTP------------EAK-----------------------------------NL 248
Cdd:cd14227 242 lLSAGTkttrffnrdTDSPYPLWRLKTPedheaetgikskEARkyifnclddmaqvnmttdlegsdmlvekadrrefiDL 321
                       330       340
                ....*....|....*....|....
gi 26051218 249 INQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14227 322 LKKMLTIDADKRITPIETLNHPFV 345
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
12-272 2.60e-16

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: 79.32  E-value: 2.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYED---IGKGAFSVVRRCVKLCTGHEYAAKIIN-TKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd06635  22 DPEKLFSDlreIGHGSFGAVYFARDVRTSEVVAIKKMSySGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAW 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGG--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ 165
Cdd:cd06635 102 LVMEYCLGSasDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIAS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQawfgFAGTPGYLSPEV---LRKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIKAGAYDFPSPEWdtv 241
Cdd:cd06635 177 PANS----FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNESPTLQSNEW--- 249
                       250       260       270
                ....*....|....*....|....*....|.
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06635 250 SDYFRNFVDSCLQKIPQDRPTSEELLKHMFV 280
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
20-204 2.84e-16

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: 78.33  E-value: 2.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELf 99
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV----DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVARE----YYSEADASHCiqQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEV----QGDQQAW 171
Cdd:cd14156  76 EELLAREelplSWREKVELAC--DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempANDPERK 153
                       170       180       190
                ....*....|....*....|....*....|...
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14156 154 LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVL 186
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
10-204 3.26e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 80.51  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   10 FTDEYQLYEDIGKGAFSVVRRC-VKLCTGHEYAAKIINTK---------------KLSARDHQKLEREARICRLLKHSNI 73
Cdd:PHA03210 146 FLAHFRVIDDLPAGAFGKIFICaLRASTEEAEARRGVNSTnqgkpkcerliakrvKAGSRAAIQLENEILALGRLNHENI 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   74 VRLHDSISEEGFHYLV-----FDLVTggelF---EDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLa 145
Cdd:PHA03210 226 LKIEEILRSEANTYMItqkydFDLYS----FmydEAFDWKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFL- 300
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  146 sKCKGAAVkLADFGLAIEVQGDQQAW-FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:PHA03210 301 -NCDGKIV-LGDFGTAMPFEKEREAFdYGWVGTVATNSPEILAGDGYCEITDIWSCGLIL 358
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
19-269 3.61e-16

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: 78.55  E-value: 3.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDS----ISEEGFHYLVFDLVT 94
Cdd:cd14030  32 EIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSwestVKGKKCIVLVTELMT 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCkgAAVKLADFGLAIEvqgdQQAWF 172
Cdd:cd14030 112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLqfLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATL----KRASF 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFA--GTPGYLSPEvLRKEAYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYdfPSPEWDTVTPEAKNLI 249
Cdd:cd14030 186 AKSviGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRRVTSGVK--PASFDKVAIPEVKEII 262
                       250       260
                ....*....|....*....|
gi 26051218 250 NQMLTINPAKRITAHEALKH 269
Cdd:cd14030 263 EGCIRQNKDERYAIKDLLNH 282
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
13-265 4.98e-16

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: 78.75  E-value: 4.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTK-------------KLSA--RDHQK--------LEREARICRLLK 69
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNapenvelalrefwALSSiqRQHPNviqleecvLQRDGLAQRMSH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  70 HSNIVRLHDSISEEG-------------FHYLVFDLVTGGELFEDIVAREYYSEADASHcIQQILEAVLHCHQMGVVHRD 136
Cdd:cd13977  81 GSSKSDLYLLLVETSlkgercfdprsacYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSF-MLQLSSALAFLHRNQIVHRD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 137 LKPENLLLASKCKGAAVKLADFGLAIEVQGD----------QQAWFGFA-GTPGYLSPEVLRKEaYGKPVDIWACGVILY 205
Cdd:cd13977 160 LKPDNILISHKRGEPILKVADFGLSKVCSGSglnpeepanvNKHFLSSAcGSDFYMAPEVWEGH-YTAKADIFALGIIIW 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 206 IlLVGYPPFWDEDQHK--LYQQIKAGAYDFP-------SPEWDTVTP---------EAKNLINQMLTINPAKRITAHE 265
Cdd:cd13977 239 A-MVERITFRDGETKKelLGTYIQQGKEIVPlgealleNPKLELQIPlkkkksmndDMKQLLRDMLAANPQERPDAFQ 315
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
49-214 6.28e-16

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: 78.04  E-value: 6.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  49 KLSARDHQKLEREARICRLLKHSNIVRLHDsISEEGFH------YLVFDLVTGGELFEDIVAREY---YSEADASHCIQQ 119
Cdd:cd14039  29 ELSVKNKDRWCHEIQIMKKLNHPNVVKACD-VPEEMNFlvndvpLLAMEYCSGGDLRKLLNKPENccgLKESQVLSLLSD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 120 ILEAVLHCHQMGVVHRDLKPENLLLaSKCKGAAV-KLADFGLAIEVqgDQQAW-FGFAGTPGYLSPEVLRKEAYGKPVDI 197
Cdd:cd14039 108 IGSGIQYLHENKIIHRDLKPENIVL-QEINGKIVhKIIDLGYAKDL--DQGSLcTSFVGTLQYLAPELFENKSYTVTVDY 184
                       170
                ....*....|....*..
gi 26051218 198 WACGVILYILLVGYPPF 214
Cdd:cd14039 185 WSFGTMVFECIAGFRPF 201
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
14-272 6.49e-16

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: 77.84  E-value: 6.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtkkLSARDHQKLEREARICRLLKH-SNIVRLHDSISEE---GFH--- 86
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTGDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKnppGMDdql 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGG---ELFEDIVAREYYSEADASHCiQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIE 163
Cdd:cd06637  85 WLVMEFCGAGsvtDLIKNTKGNTLKEEWIAYIC-REILRGLSHLHQHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQAWFGFAGTPGYLSPEVLRKE-----AYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYDFPSPE 237
Cdd:cd06637 161 LDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDmHPMRALFLIPRNPAPRLKSKK 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 238 WdtvTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06637 241 W---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
10-271 1.76e-15

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: 76.85  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  10 FTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL---SARDHQKLEREARIC--RLLKHSNIVRLHDS---IS 81
Cdd:cd14136   8 YNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHyteAALDEIKLLKCVREAdpKDPGREHVVQLLDDfkhTG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  82 EEGFHY-LVFDlVTGGELFEDIVAREYysEADASHC----IQQILEAVLHCH-QMGVVHRDLKPENLLLASKckGAAVKL 155
Cdd:cd14136  88 PNGTHVcMVFE-VLGPNLLKLIKRYNY--RGIPLPLvkkiARQVLQGLDYLHtKCGIIHTDIKPENVLLCIS--KIEVKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 156 ADFGLAI--------EVQGDQqawfgfagtpgYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF---------WDED 218
Cdd:cd14136 163 ADLGNACwtdkhfteDIQTRQ-----------YRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphsgedysRDED 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 219 Q-----------------------------------HKLY----QQIKAGAYDFPSPEWDTVTpeakNLINQMLTINPAK 259
Cdd:cd14136 232 HlaliiellgriprsiilsgkysreffnrkgelrhiSKLKpwplEDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEK 307
                       330
                ....*....|..
gi 26051218 260 RITAHEALKHPW 271
Cdd:cd14136 308 RATAAQCLQHPW 319
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
12-281 6.12e-15

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: 74.77  E-value: 6.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRcvklcTGHEYAAKIINTKKLSA----RDHQKLEREARICRLLKHS-NIVRLHDSISEEG-- 84
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDK-----MRHVPTGTIMAVKRIRAtvnsQEQKRLLMDLDISMRSVDCpYTVTFYGALFREGdv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 -------------FHYLVFDlvTGGELFEDIVAREYYSeadashciqqILEAVLHCH-QMGVVHRDLKPENLLLAskcKG 150
Cdd:cd06617  76 wicmevmdtsldkFYKKVYD--KGLTIPEDILGKIAVS----------IVKALEYLHsKLSVIHRDVKPSNVLIN---RN 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 151 AAVKLADFG----LAIEVQGDQQawfgfAGTPGYLSPEVLRKE----AYGKPVDIWACGVILYILLVGYPPFwdEDQHKL 222
Cdd:cd06617 141 GQVKLCDFGisgyLVDSVAKTID-----AGCKPYMAPERINPElnqkGYDVKSDVWSLGITMIELATGRFPY--DSWKTP 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 223 YQQIKAGAYDfPSPEW--DTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ----RSTVASM 281
Cdd:cd06617 214 FQQLKQVVEE-PSPQLpaEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELhlskNTDVASF 277
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
13-205 6.42e-15

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: 74.41  E-value: 6.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCvKLCTGHEYAAKIINTKKLSARDhqkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05059   5 ELTFLKELGSGQFGVVHLG-KWRGKIDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVARE--YYSEADASHCiQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGDQQA 170
Cdd:cd05059  81 MANGCLLNYLRERRgkFQTEQLLEMC-KDVCEAMEYLESNGFIHRDLAARNCLVGEQN---VVKVSDFGLARYVLDDEYT 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 26051218 171 WFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY 205
Cdd:cd05059 157 SSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMW 192
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
13-270 7.13e-15

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: 74.31  E-value: 7.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRcvklctgHEYAAKIINTKKLsaRDH----QKLEREARICRLLKHSNIVRLHDSISEEGFHYL 88
Cdd:cd05039   7 DLKLGELIGKGEFGDVML-------GDYRGQKVAVKCL--KDDstaaQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFEDIVAREyyseadaSHCI---QQILEAVLHCHQM------GVVHRDLKPENLLLASKCkgaAVKLADFG 159
Cdd:cd05039  78 VTEYMAKGSLVDYLRSRG-------RAVItrkDQLGFALDVCEGMeyleskKFVHRDLAARNVLVSEDN---VAKVSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 160 LAIEVQGDQQA------WfgfagtpgyLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYD 232
Cdd:cd05039 148 LAKEASSNQDGgklpikW---------TAPEALREKKFSTKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPHVEKG-YR 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26051218 233 FPSPEwdTVTPEAKNLINQMLTINPAKRIT---AHEALKHP 270
Cdd:cd05039 218 MEAPE--GCPPEVYKVMKNCWELDPAKRPTfkqLREKLEHI 256
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
14-272 9.79e-15

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: 74.27  E-value: 9.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklsarDHQKLEREARICRLLK---HSNIVRLHDSI---SEEGFH- 86
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVT-----EDEEEEIKLEINMLKKyshHRNIATYYGAFikkSPPGHDd 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 --YLVFDLVTGGELfEDIVAR---EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLA 161
Cdd:cd06636  93 qlWLVMEFCGAGSV-TDLVKNtkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 162 IEVQGDQQAWFGFAGTPGYLSPEVLRKE-----AYGKPVDIWACGVILYILLVGYPPFWD-EDQHKLYQQIKAGAYDFPS 235
Cdd:cd06636 169 AQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDmHPMRALFLIPRNPPPKLKS 248
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 236 PEWdtvTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06636 249 KKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
4-270 2.26e-14

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: 73.17  E-value: 2.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   4 TVTCTRFTDEyqlyEDIGKGAFSVVRRCVklctgHEYAAKIINTKKLSA----RDHQKLERE------ARICrllkhSNI 73
Cdd:cd06616   2 EFTAEDLKDL----GEIGRGAFGTVNKML-----HKPSGTIMAVKRIRStvdeKEQKRLLMDldvvmrSSDC-----PYI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  74 VRLHDSISEEG---------------FHYLVFDlVTGGELFEDIVAREYYSEADASHCIQQILEavlhchqmgVVHRDLK 138
Cdd:cd06616  68 VKFYGALFREGdcwicmelmdisldkFYKYVYE-VLDSVIPEEILGKIAVATVKALNYLKEELK---------IIHRDVK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 139 PENLLLAskcKGAAVKLADFGLAIEVQgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDI----WACGVILYILLVG-YP- 212
Cdd:cd06616 138 PSNILLD---RNGNIKLCDFGISGQLV-DSIAKTRDAGCRPYMAPERIDPSASRDGYDVrsdvWSLGITLYEVATGkFPy 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 213 PFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd06616 214 PKWNSVFDQLTQVVKGDPPILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHP 271
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
12-271 2.43e-14

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: 73.90  E-value: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAA-KIIntkklsaRDHQKLEREARI-CRLLKHSN---------IVRLHDSI 80
Cdd:cd14215  12 ERYEIVSTLGEGTFGRVVQCIDHRRGGARVAlKII-------KNVEKYKEAARLeINVLEKINekdpenknlCVQMFDWF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  81 SEEGFHYLVFDLVtGGELFEDIVAREY--YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK----------- 147
Cdd:cd14215  85 DYHGHMCISFELL-GLSTFDFLKENNYlpYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSdyeltynlekk 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 -----CKGAAVKLADFGLAievQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL 222
Cdd:cd14215 164 rdersVKSTAIRVVDFGSA---TFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 223 YQQIKAGAYDFPSP----------------EWDTVTPEAK------------------------NLINQMLTINPAKRIT 262
Cdd:cd14215 241 LAMMERILGPIPSRmirktrkqkyfyhgrlDWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLT 320

                ....*....
gi 26051218 263 AHEALKHPW 271
Cdd:cd14215 321 LAAALKHPF 329
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
12-301 3.86e-14

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: 72.75  E-value: 3.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYED---IGKGAFSVVRRCVKLCTGHEYAAKIIN-TKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd06634  12 DPEKLFSDlreIGHGSFGAVYFARDVRNNEVVAIKKMSySGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAW 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGG--ELFEdiVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ 165
Cdd:cd06634  92 LVMEYCLGSasDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP---GLVKLGDFGSASIMA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQawfgFAGTPGYLSPEV---LRKEAYGKPVDIWACGVILYILLVGYPPFWDED-QHKLYQQIKAGAYDFPSPEWdtv 241
Cdd:cd06634 167 PANS----FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNaMSALYHIAQNESPALQSGHW--- 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 242 TPEAKNLINQMLTINPAKRITAHEALKHPWVC-QRSTVASMMHRQETVECLKKFN--ARRKLK 301
Cdd:cd06634 240 SEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLrERPPTVIMDLIQRTKDAVRELDnlQYRKMK 302
pknD PRK13184
serine/threonine-protein kinase PknD;
14-268 3.96e-14

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 74.81  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINtKKLS--ARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIR-EDLSenPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   92 LVTGGELFE--------DIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGL 160
Cdd:PRK13184  83 YIEGYTLKSllksvwqkESLSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLG---LFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  161 AI--EVQGDQQAWFGF----------------AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL 222
Cdd:PRK13184 160 AIfkKLEEEDLLDIDVdernicyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 26051218  223 Y--QQIkagaydfPSPE----WDTVTPEAKNLINQMLTINPAKRITAHEALK 268
Cdd:PRK13184 240 SyrDVI-------LSPIevapYREIPPFLSQIAMKALAVDPAERYSSVQELK 284
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
14-272 4.53e-14

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: 72.87  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKlerEARICRLLKHS-----NIVRLHDSISEEGFHYL 88
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI---EVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGgELFeDIVAREYYSEADASH---CIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGLAIEV 164
Cdd:cd14211  78 VFEMLEQ-NLY-DFLKQNKFSPLPLKYirpILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 165 QGDQQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYP--PFWDE-DQ-------------HKLYQQIKA 228
Cdd:cd14211 156 SKAVCS--TYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPlyPGSSEyDQiryisqtqglpaeHLLNAATKT 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 229 G-----AYDFPSPEWDTVTPEAK-----------------------------------------------NLINQMLTIN 256
Cdd:cd14211 234 SrffnrDPDSPYPLWRLKTPEEHeaetgikskearkyifnclddmaqvngpsdlegsellaekadrrefiDLLKRMLTID 313
                       330
                ....*....|....*.
gi 26051218 257 PAKRITAHEALKHPWV 272
Cdd:cd14211 314 QERRITPGEALNHPFV 329
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
5-227 4.53e-14

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: 73.20  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   5 VTCTrFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKlerEARICRLLKHSN-----IVRLHDS 79
Cdd:cd14228   9 ILCS-MTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQI---EVSILSRLSSENadeynFVRSYEC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  80 ISEEGFHYLVFDLVTggELFEDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKL 155
Cdd:cd14228  85 FQHKNHTCLVFEMLE--QNLYDFLKQNKFSPLPLKYIrpiLQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKV 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 156 ADFGLAIEVQgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQhklYQQIK 227
Cdd:cd14228 163 IDFGSASHVS--KAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASE---YDQIR 229
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
20-236 5.94e-14

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: 71.54  E-value: 5.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd05063  13 IGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDflSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LfeDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd05063  93 L--DKYLRDHdgeFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLE---CKVSDFGLSRVLEDDPEGTYTT 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 175 AGTP---GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSP 236
Cdd:cd05063 168 SGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAINDG-FRLPAP 232
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
12-229 7.07e-14

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member 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, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk 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: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 71.13  E-value: 7.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLcTGHEYAAKIINTKKLSARDhqkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWL-NKDKVAIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVARE--YYSEADASHCIqQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQq 169
Cdd:cd05112  80 FMEHGCLSDYLRTQRglFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLVG---ENQVVKVSDFGMTRFVLDDQ- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 170 aWFGFAGTP---GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05112 155 -YTSSTGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWeVFSEGKIPYENRSNSEVVEDINAG 217
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
13-214 8.37e-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: 71.20  E-value: 8.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCvklcTGH-EYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHyLVFD 91
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRG----KWHgDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFA-IITQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI---EVQGD 167
Cdd:cd14150  76 WCEGSSLYRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLH---EGLTVKIGDFGLATvktRWSGS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGfAGTPGYLSPEVLRKE---AYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14150 153 QQVEQP-SGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
16-281 1.15e-13

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: 70.91  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  16 LYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKK--LSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFDLV 93
Cdd:cd05056  10 LGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKncTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPV-WIVMELA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK-CkgaaVKLADFGLAIEVqgDQQAW 171
Cdd:cd05056  89 PLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPdC----VKLGDFGLSRYM--EDESY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 FGFAGTP---GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGAyDFPSPEwdTVTPEAKN 247
Cdd:cd05056 163 YKASKGKlpiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIENGE-RLPMPP--NCPPTLYS 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 248 LINQMLTINPAKRITAHEAlkhpwVCQRSTVASM 281
Cdd:cd05056 240 LMTKCWAYDPSKRPRFTEL-----KAQLSDILQE 268
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
117-266 1.63e-13

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: 70.99  E-value: 1.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAV-KLADFG--LAIEVQGDQ----QAWFGFAGTPGYLSPEVLR-- 187
Cdd:cd14018 144 ILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFGccLADDSIGLQlpfsSWYVDRGGNACLMAPEVSTav 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 188 -----KEAYGKpVDIWACGVILYILLVGYPPFWDEDQHKL----YQQIKAGAydFPspewDTVTPEAKNLINQMLTINPA 258
Cdd:cd14018 224 pgpgvVINYSK-ADAWAVGAIAYEIFGLSNPFYGLGDTMLesrsYQESQLPA--LP----SAVPPDVRQVVKDLLQRDPN 296

                ....*...
gi 26051218 259 KRITAHEA 266
Cdd:cd14018 297 KRVSARVA 304
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
13-268 2.02e-13

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: 70.16  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRcvKLCTGH-EYAAKIIntKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd05148   7 EFTLERKLGSGYFGEVWE--GLWKNRvRVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSeADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQ 168
Cdd:cd05148  83 LMEKGSLLAFLRSPEGQV-LPVASLIDmacQVAEGMAYLEEQNSIHRDLAARNILVG---EDLVCKVADFGLARLIKEDV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 qawfgfagtpgYLS-----------PEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSP 236
Cdd:cd05148 159 -----------YLSsdkkipykwtaPEAASHGTFSTKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQITAG-YRMPCP 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 237 EwdTVTPEAKNLINQMLTINPAKRITAHeALK 268
Cdd:cd05148 227 A--KCPQEIYKIMLECWAAEPEDRPSFK-ALR 255
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
18-260 2.13e-13

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. 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. Fes subfamily proteins 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. 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 tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 69.78  E-value: 2.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKkLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFEDIvaREYYSEADASHCIQQILEA---VLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ-QAWFG 173
Cdd:cd05041  80 LLTFL--RKKGARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGEN---NVLKISDFGMSREEEDGEyTVSDG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 174 FAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEwdtVTPEA-KNLIN 250
Cdd:cd05041 155 LKQIPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIESG-YRMPAPE---LCPEAvYRLML 230
                       250
                ....*....|
gi 26051218 251 QMLTINPAKR 260
Cdd:cd05041 231 QCWAYDPENR 240
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
21-214 2.91e-13

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: 69.22  E-value: 2.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  21 GKGAFSVVRRCVKLCTGHEYAAKIINtkklsardhqKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFE 100
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLL----------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 101 DIVAREyYSEADASHCIQQILEAVLHCHQM------GVVHRDLKPENLLLASKckgAAVKLADFGLAIEVqgDQQAWFGF 174
Cdd:cd14060  72 YLNSNE-SEEMDMDQIMTWATDIAKGMHYLhmeapvKVIHRDLKSRNVVIAAD---GVLKICDFGASRFH--SHTTHMSL 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 26051218 175 AGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14060 146 VGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
31-205 3.64e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 71.08  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   31 CVKLCTGHEYAAKIIntkkLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGgELFEDIVAR-EYYS 109
Cdd:PHA03211 184 CVFESSHPDYPQRVV----VKAGWYASSVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGARlRPLG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  110 EADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQ--AWFGFAGTPGYLSPEVLR 187
Cdd:PHA03211 259 LAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGP---EDICLGDFGAACFARGSWStpFHYGIAGTVDTNAPEVLA 335
                        170
                 ....*....|....*...
gi 26051218  188 KEAYGKPVDIWACGVILY 205
Cdd:PHA03211 336 GDPYTPSVDIWSAGLVIF 353
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
20-227 4.81e-13

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: 68.82  E-value: 4.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKiinTKKLSARDhQKLEREARICRLLKHSNIV-RLHDSISEEGFHYLVFDLVtGGEL 98
Cdd:cd14017   8 IGGGGFGEIYKVRDVVDGEEVAMK---VESKSQPK-QVLKMEVAVLKKLQGKPHFcRLIGCGRTERYNYIVMTLL-GPNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  99 FEdiVAREY----YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLL---ASKCKgaAVKLADFGLA---IEVQGD- 167
Cdd:cd14017  83 AE--LRRSQprgkFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDER--TVYILDFGLArqyTNKDGEv 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 168 ----QQAWfGFAGTPGYLSPEVLRKEAYGKPVDIWAcgvILYILL---VGYPPFWDEDQHKLYQQIK 227
Cdd:cd14017 159 erppRNAA-GFRGTVRYASVNAHRNKEQGRRDDLWS---WFYMLIefvTGQLPWRKLKDKEEVGKMK 221
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
58-270 6.66e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 69.87  E-value: 6.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   58 LEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDL 137
Cdd:PHA03207 133 PGREIDILKTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  138 KPENLLLASkcKGAAVkLADFGLAIEVQG--DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFW 215
Cdd:PHA03207 212 KTENIFLDE--PENAV-LGDFGAACKLDAhpDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLF 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  216 ----DEDQHKLYQQIKA---GAYDFPSPEWDTVTPEAKN--------------------------LINQMLTINPAKRIT 262
Cdd:PHA03207 289 gkqvKSSSSQLRSIIRCmqvHPLEFPQNGSTNLCKHFKQyaivlrppytippvirkygmhmdveyLIAKMLTFDQEFRPS 368

                 ....*...
gi 26051218  263 AHEALKHP 270
Cdd:PHA03207 369 AQDILSLP 376
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
13-269 6.70e-13

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: 68.47  E-value: 6.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRrcVKLCTGHEYAAKIINTKKLSardhQKLEREARICRLLKHSNIVRLHDSISEE-GFHYLVFD 91
Cdd:cd05082   7 ELKLLQTIGKGEFGDVM--LGDYRGNKVAVKCIKNDATA----QAFLAEASVMTQLRHSNLVQLLGVIVEEkGGLYIVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYySEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQ 168
Cdd:cd05082  81 YMAKGSLVDYLRSRGR-SVLGGDCLLKfslDVCEAMEYLEGNNFVHRDLAARNVLVSED---NVAKVSDFGLTKEASSTQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 QAwfgfAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPewDTVTPEAK 246
Cdd:cd05082 157 DT----GKLPvKWTAPEALREKKFSTKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPRVEKG-YKMDAP--DGCPPAVY 229
                       250       260
                ....*....|....*....|....*.
gi 26051218 247 NLINQMLTINPAKRIT---AHEALKH 269
Cdd:cd05082 230 DVMKNCWHLDAAMRPSflqLREQLEH 255
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
20-263 1.01e-12

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: 67.67  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKlcTGHEYAAKIINtKKLSARdhqKLEREARICRLLKHSNIVRLHDSiseeGFH--YLVFDLVTGGE 97
Cdd:cd14068   2 LGDGGFGSVYRAVY--RGEDVAVKIFN-KHTSFR---LLRQELVVLSHLHHPSLVALLAA----GTAprMLVMELAPKGS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LfEDIVAREYYS-EADASHCIQ-QILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAV--KLADFGLAIEV--QGDQQAw 171
Cdd:cd14068  72 L-DALLQQDNASlTRTLQHRIAlHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYCcrMGIKTS- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 172 fgfAGTPGYLSPEVLRKE-AYGKPVDIWACGVILYILLVG---------YPPFWDE--DQHKLYQQIKagayDFPSPEWd 239
Cdd:cd14068 150 ---EGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTCgeriveglkFPNEFDElaIQGKLPDPVK----EYGCAPW- 221
                       250       260
                ....*....|....*....|....
gi 26051218 240 tvtPEAKNLINQMLTINPAKRITA 263
Cdd:cd14068 222 ---PGVEALIKDCLKENPQCRPTS 242
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
20-214 1.04e-12

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: 67.91  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVkLCTGHEYAAKIINTKKLSARDHQkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELF 99
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 100 EDIVAREYYSEADASHCIQQI-LEAV-----LHCH-QMGVVHRDLKPENLLLASKCKGaavKLADFGLA-IEVQGDQQAW 171
Cdd:cd14664  79 ELLHSRPESQPPLDWETRQRIaLGSArglayLHHDcSPLIIHRDVKSNNILLDEEFEA---HVADFGLAkLMDDKDSHVM 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 26051218 172 FGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14664 156 SSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
19-208 1.09e-12

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: 68.18  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCvklC-------TGHEYAAKIINT--KKLSARDhqkLEREARICRLLKHSNIVRLhDSISEEGF---H 86
Cdd:cd05038  11 QLGEGHFGSVELC---RydplgdnTGEQVAVKSLQPsgEEQHMSD---FKREIEILRTLDHEYIVKY-KGVCESPGrrsL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  87 YLVFDLVTGGELfeDIVAREYYSEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIE 163
Cdd:cd05038  84 RLIMEYLPSGSL--RDYLQRHRDQIDLKRLLlfaSQICKGMEYLGSQRYIHRDLAARNILVESE---DLVKISDFGLAKV 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQawFGFAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd05038 159 LPEDKE--YYYVKEPGespifWYAPECLRESRFSSASDVWSFGVTLYELF 206
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
50-268 1.32e-12

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 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 PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 67.66  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  50 LSARDHQKLEREARIcRLLKHSNIVRLHDSISEEGFHYLVFDLVTGgELFEDIVAREYYSEADASHCIQQILEAVLHCHQ 129
Cdd:cd13980  38 LPLRSYKQRLEEIRD-RLLELPNVLPFQKVIETDKAAYLIRQYVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHK 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 130 MGVVHRDLKPENLLLASkckGAAVKLADFG--LAIEVQGDQQAWFG-FAGTPG----YLSPE------------VLRKEA 190
Cdd:cd13980 116 RGVCHGDIKTENVLVTS---WNWVYLTDFAsfKPTYLPEDNPADFSyFFDTSRrrtcYIAPErfvdaltldaesERRDGE 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 191 YGKPVDIWACG-VILYILLVGYPPFwDEDQHKLYqqiKAGAYDfPSPEWDTVTPE-AKNLINQMLTINPAKRITAHEALK 268
Cdd:cd13980 193 LTPAMDIFSLGcVIAELFTEGRPLF-DLSQLLAY---RKGEFS-PEQVLEKIEDPnIRELILHMIQRDPSKRLSAEDYLK 267
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
20-217 1.76e-12

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: 67.52  E-value: 1.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKlctgheyAAKIINTKKLSARDH-------QKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14158  23 LGEGGFGVVFKGYI-------NDKNVAVKKLAAMVDistedltKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREY---YSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd14158  96 MPNGSLLDRLACLNDtppLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLD---ETFVPKISDFGLARASEKFSQ 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFG--FAGTPGYLSPEVLRKEAYGKpVDIWACGVILYILLVGYPPFwDE 217
Cdd:cd14158 173 TIMTerIVGTTAYMAPEALRGEITPK-SDIFSFGVVLLEIITGLPPV-DE 220
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
13-270 1.77e-12

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: 67.43  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKiiNTKKLSA--RDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLV 89
Cdd:cd14051   1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIK--KSKKPVAgsVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDI----VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASK------------CKGAA- 152
Cdd:cd14051  79 NEYCNGGSLADAIseneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTpnpvsseeeeedFEGEEd 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 153 --------VKLADFGLAIEV------QGDQQawfgfagtpgYLSPEVLRKEAYGKP-VDIWACGVILYILLVGYP-PFWD 216
Cdd:cd14051 159 npesnevtYKIGDLGHVTSIsnpqveEGDCR----------FLANEILQENYSHLPkADIFALALTVYEAAGGGPlPKNG 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 217 EDQHKlyqqIKAGAYdfpsPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14051 229 DEWHE----IRQGNL----PPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
14-212 1.79e-12

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: 68.13  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsaRDHQKLEREARI-----CRLLKHS----NIVRLHDSISEEG 84
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL-------KNHPSYARQGQIevgilARLSNENadefNFVRAYECFQHRN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTggELFEDIVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGA-AVKLADFGL 160
Cdd:cd14229  75 HTCLVFEMLE--QNLYDFLKQNKFSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 161 AIEVQgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYP 212
Cdd:cd14229 153 ASHVS--KTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 202
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
16-229 2.47e-12

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: 67.11  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  16 LYEDIGKGAFSVVRR--CVKLCTGHEYAAKIINTKKLSARD--HQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd05049   9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPdaRKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDI--------------VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLAD 157
Cdd:cd05049  89 YMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNL---VVKIGD 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 158 FGLAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05049 166 FGMSRDIySTDYYRVGGHTMLPiRWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQLSNTEVIECITQG 240
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
18-205 2.67e-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: 67.08  E-value: 2.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCvKLcTGHEYAAKIintkkLSARDHQKLEREARICR--LLKHSNIVRL----HDSISEEGFHYLVFD 91
Cdd:cd13998   1 EVIGKGRFGEVWKA-SL-KNEPVAVKI-----FSSRDKQSWFREKEIYRtpMLKHENILQFiaadERDTALRTELWLVTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCH---------QMGVVHRDLKPENLLLasKCKGAAVkLADFGLAI 162
Cdd:cd13998  74 FHPNGSL*-DYLSLHTIDWVSLCRLALSVARGLAHLHseipgctqgKPAIAHRDLKSKNILV--KNDGTCC-IADFGLAV 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 163 EVQG----DQQAWFGFAGTPGYLSPEVL-------RKEAYgKPVDIWACGVILY 205
Cdd:cd13998 150 RLSPstgeEDNANNGQVGTKRYMAPEVLegainlrDFESF-KRVDIYAMGLVLW 202
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
20-237 2.98e-12

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, 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. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 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: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 66.72  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKL----EREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05046  13 LGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDENLqsefRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADAS------------HCIQQILEAVLHCHqmgVVHRDLKPENLLLASKCKgaaVKLADFGLAIE 163
Cdd:cd05046  93 GDLKQFLRATKSKDEKLKPpplstkqkvalcTQIALGMDHLSNAR---FVHRDLAARNCLVSSQRE---VKVSLLSLSKD 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 164 VQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPE 237
Cdd:cd05046 167 VYNSEYYKLRNALIPlRWLAPEAVQEDDFSTKSDVWSFGVLMWeVFTQGELPFYGLSDEEVLNRLQAGKLELPVPE 242
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
13-229 6.62e-12

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) 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. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk 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: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 65.65  E-value: 6.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRrCVKLCTGHEYAAKIINTKKLSARDHQKlerEARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05114   5 ELTFMKELGSGLFGVVR-LGKWRAQYKVAIKAIREGAMSEEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAREYYSEADA--SHCiQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGDQQA 170
Cdd:cd05114  81 MENGCLLNYLRQRRGKLSRDMllSMC-QDVCEGMEYLERNNFIHRDLAARNCLVNDTG---VVKVSDFGMTRYVLDDQYT 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 171 WFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05114 157 SSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRG 217
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
45-237 7.03e-12

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: 65.45  E-value: 7.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  45 INTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFeDIVAREYYSEADASHCIQ---QIL 121
Cdd:cd05072  36 VKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL-DFLKSDEGGKVLLPKLIDfsaQIA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 122 EAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWAC 200
Cdd:cd05072 115 EGMAYIERKNYIHRDLRAANVLVS---ESLMCKIADFGLARVIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSF 191
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 26051218 201 GVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:cd05072 192 GILLYeIVTYGKIPYPGMSNSDVMSALQRG-YRMPRME 228
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
12-237 9.48e-12

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. 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 Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 65.09  E-value: 9.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVklCTGHEYAAkiINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFD 91
Cdd:cd05070   9 ESLQLIKRLGNGQFGEVWMGT--WNGNTKVA--IKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPI-YIVTE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVARE--YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAIEVQGDQQ 169
Cdd:cd05070  84 YMSKGSLLDFLKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN---GLICKIADFGLARLIEDNEY 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 170 AWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILYILLV-GYPPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:cd05070 161 TARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMPCPQ 229
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
45-262 1.21e-11

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. 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 Yes 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 (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 65.09  E-value: 1.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  45 INTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFDLVTGGELFEdivareYYSEADASHC-------- 116
Cdd:cd05069  41 IKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPI-YIVTEFMGKGSLLD------FLKEGDGKYLklpqlvdm 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPV 195
Cdd:cd05069 114 AAQIADGMAYIERMNYIHRDLRAANILVGDNL---VCKIADFGLARLIEDNEYTARQGAKFPiKWTAPEAALYGRFTIKS 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 196 DIWACGVILYILLV-GYPPFWDEDQHKLYQQIKAGaYDFPSPEWdtvTPEA-KNLINQMLTINPAKRIT 262
Cdd:cd05069 191 DVWSFGILLTELVTkGRVPYPGMVNREVLEQVERG-YRMPCPQG---CPESlHELMKLCWKKDPDERPT 255
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
115-271 1.34e-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: 64.96  E-value: 1.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 115 HCIQQILEAVLHCHQMGVVHRDLKPENLLLASkcKGAAVKLADFGLAIEvQGDQQAwfGFAGTPGYLSPEVLRKEAYGK- 193
Cdd:cd14020 114 HCARDVLEALAFLHHEGYVHADLKPRNILWSA--EDECFKLIDFGLSFK-EGNQDV--KYIQTDGYRAPEAELQNCLAQa 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 194 ----------PVDIWACGVILYILLVGYppfwdedqhKLYQQIKagaydfpSPEWDT---------------VTP----- 243
Cdd:cd14020 189 glqsetectsAVDLWSLGIVLLEMFSGM---------KLKHTVR-------SQEWKDnssaiidhifasnavVNPaipay 252
                       170       180
                ....*....|....*....|....*...
gi 26051218 244 EAKNLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd14020 253 HLRDLIKSMLHNDPGKRATAEAALCSPF 280
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
20-208 1.59e-11

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: 64.53  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGhEYAAKIINTKKL---SARDHQKLEREARICRLLKHSNIVRLHD---SISEEGFHyLVFDLV 93
Cdd:cd05081  12 LGKGNFGSVELCRYDPLG-DNTGALVAVKQLqhsGPDQQRDFQREIQILKALHSDFIVKYRGvsyGPGRRSLR-LVMEYL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELfedivaREYYSE----ADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQG 166
Cdd:cd05081  90 PSGCL------RDFLQRhrarLDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVESE---AHVKIADFGLAKLLPL 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 167 DQQAWFgfAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd05081 161 DKDYYV--VREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
61-262 1.67e-11

Catalytic domain of a subset 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. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. 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. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-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: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 64.17  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  61 EARICRLLKHSNIVRLHDSISEEGFhYLVFDLVTGGELFedivarEYYSEADASHC--------IQQILEAVLHCHQMGV 132
Cdd:cd14203  40 EAQIMKKLRHDKLVQLYAVVSEEPI-YIVTEFMSKGSLL------DFLKDGEGKYLklpqlvdmAAQIASGMAYIERMNY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 133 VHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVlrkEAYGK---PVDIWACGVILYILL 208
Cdd:cd14203 113 IHRDLRAANILVG---DNLVCKIADFGLARLIEDNEYTARQGAKFPiKWTAPEA---ALYGRftiKSDVWSFGILLTELV 186
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26051218 209 V-GYPPFWDEDQHKLYQQIKAGaYDFPSPEwdTVTPEAKNLINQMLTINPAKRIT 262
Cdd:cd14203 187 TkGRVPYPGMNNREVLEQVERG-YRMPCPP--GCPESLHELMCQCWRKDPEERPT 238
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
18-208 1.71e-11

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: 64.65  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCvKLCTGHEYAAKIINTKKL--SARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFH--YLVFDL 92
Cdd:cd14205  10 QQLGKGNFGSVEMC-RYDPLQDNTGEVVAVKKLqhSTEEHlRDFEREIEILKSLQHDNIVKYKGVCYSAGRRnlRLIMEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELfedivaREYYSEA----DASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQ 165
Cdd:cd14205  89 LPYGSL------RDYLQKHkeriDHIKLLQytsQICKGMEYLGTKRYIHRDLATRNILVENENR---VKIGDFGLTKVLP 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 166 GDQQAWFgfAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd14205 160 QDKEYYK--VKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
20-204 1.78e-11

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: 64.19  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSvvrRCVKLCtgHEYAAKIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14222   1 LGKGFFG---QAIKVT--HKATGKVMVMKELIRCDEETQKtflTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLasKCKGAAVkLADFGLAIEV------------ 164
Cdd:cd14222  76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI--KLDKTVV-VADFGLSRLIveekkkpppdkp 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 165 --------QGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14222 153 ttkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVL 200
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
117-272 1.88e-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: 1.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLASKCKgaAVKLADFGLAIEVQ-GDQQAWFGFAGTPGYLSPE--VLRKEA--- 190
Cdd:cd14013 126 MRQILVALRKLHSTGIVHRDVKPQNIIVSEGDG--QFKIIDLGAAADLRiGINYIPKEFLLDPRYAPPEqyIMSTQTpsa 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 191 ---------------YGKP--VDIWACGVILyiLLVGYPPFWDEDQHKLY-QQIKAGAYDFpsPEWDTVTPEAKN----- 247
Cdd:cd14013 204 ppapvaaalspvlwqMNLPdrFDMYSAGVIL--LQMAFPNLRSDSNLIAFnRQLKQCDYDL--NAWRMLVEPRASadlre 279
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 26051218 248 --------------LINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd14013 280 gfeildlddgagwdLVTKLIRYKPRGRLSASAALAHPYF 318
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
13-262 3.17e-11

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: 63.52  E-value: 3.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRcvklctGH---EYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHR------GRwhgDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFEDIvaREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLaSKCKgaaVKLADFGL-AIEVQ 165
Cdd:cd14063  75 TSLCKGRTLYSLI--HERKEKFDFNktvQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGR---VVITDFGLfSLSGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 166 GDQQAWFGFAGTPG----YLSPEVLRKEAYGKPV----------DIWACGVILYILLVGYPPFwdEDQH---KLYQqikA 228
Cdd:cd14063 149 LQPGRREDTLVIPNgwlcYLAPEIIRALSPDLDFeeslpftkasDVYAFGTVWYELLAGRWPF--KEQPaesIIWQ---V 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 26051218 229 GAYDFPSPEWDTVTPEAKNLINQMLTINPAKRIT 262
Cdd:cd14063 224 GCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPT 257
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
18-237 3.21e-11

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: 63.55  E-value: 3.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAF-SVVRRCVKLcTGHEYAAKIINTKKLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05033  10 KVIGGGEFgEVCSGSLKL-PGKKEIDVAIKTLKSGYSDKQRLDflTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEdivareYYSEADASHCIQQILE-------AVLHCHQMGVVHRDLKPENLLLASK--CkgaavKLADFGLAIEVQ 165
Cdd:cd05033  89 NGSLDK------FLRENDGKFTVTQLVGmlrgiasGMKYLSEMNYVHRDLAARNILVNSDlvC-----KVSDFGLSRRLE 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 166 GDQQAWfgfaGTPG------YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:cd05033 158 DSEATY----TTKGgkipirWTAPEAIAYRKFTSASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAVEDG-YRLPPPM 231
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
20-205 4.92e-11

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: 63.53  E-value: 4.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcvKLCTGHEYAAKIintkkLSARDHQKLEREARICRL--LKHSNIVRLH---DSISEEGF--HYLVFDL 92
Cdd:cd14054   3 IGQGRYGTVWK--GSLDERPVAVKV-----FPARHRQNFQNEKDIYELplMEHSNILRFIgadERPTADGRmeYLLVLEY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIvaREYYSEADAS----HCIQQILeAVLH-------CHQMGVVHRDLKPENLLLasKCKGAAVkLADFGLA 161
Cdd:cd14054  76 APKGSLCSYL--RENTLDWMSScrmaLSLTRGL-AYLHtdlrrgdQYKPAIAHRDLNSRNVLV--KADGSCV-ICDFGLA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 162 IEVQGDQQAWFGF----------AGTPGYLSPEVLRK-------EAYGKPVDIWACGVILY 205
Cdd:cd14054 150 MVLRGSSLVRGRPgaaenasiseVGTLRYMAPEVLEGavnlrdcESALKQVDVYALGLVLW 210
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
57-237 6.12e-11

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: 62.33  E-value: 6.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  57 KLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIvaREYYSEADASHCIQQILEA---VLHCHQMGVV 133
Cdd:cd05085  39 KFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFL--RKKKDELKTKQLVKFSLDAaagMAYLESKNCI 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 134 HRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGY 211
Cdd:cd05085 117 HRDLAARNCLVG---ENNALKISDFGMSRQEDDGVYSSSGLKQIPiKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGV 193
                       170       180
                ....*....|....*....|....*.
gi 26051218 212 PPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:cd05085 194 CPYPGMTNQQAREQVEKG-YRMSAPQ 218
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
18-214 1.01e-10

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: 62.34  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSvvrrcvKLCTGHEYA------AKIINTKKLSARDH----QKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd05091  12 EELGEDRFG------KVYKGHLFGtapgeqTQAVAIKTLKDKAEgplrEEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELFEDIVAREYYSE----------------ADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKga 151
Cdd:cd05091  86 MIFSYCSHGDLHEFLVMRSPHSDvgstdddktvkstlepADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN-- 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 152 aVKLADFGLAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPF 214
Cdd:cd05091 164 -VKISDLGLFREVyAADYYKLMGNSLLPiRWMSPEAIMYGKFSIDSDIWSYGVVLWeVFSYGLQPY 228
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
14-271 1.11e-10

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: 62.56  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKL-CTGHEYAAKIIntkKLSARDHQKLEREARIcrlLKHSN---------IVRLHDSISEE 83
Cdd:cd14213  14 YEIVDTLGEGAFGKVVECIDHkMGGMHVAVKIV---KNVDRYREAARSEIQV---LEHLNttdpnstfrCVQMLEWFDHH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  84 GFHYLVFDLVtgGELFEDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASK------------- 147
Cdd:cd14213  88 GHVCIVFELL--GLSTYDFIKENSFLPFPIDHIRNmayQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkynpkmkrd 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 148 ---CKGAAVKLADFGLAIEvqgDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDED------ 218
Cdd:cd14213 166 ertLKNPDIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDskehla 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 219 ----------QHKLYQQIKAGAYDFPSPEWDTVTPEAK------------------------NLINQMLTINPAKRITAH 264
Cdd:cd14213 243 mmerilgplpKHMIQKTRKRKYFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLD 322

                ....*..
gi 26051218 265 EALKHPW 271
Cdd:cd14213 323 EALKHPF 329
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
12-214 1.11e-10

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: 62.02  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKL----SARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHY 87
Cdd:cd05036   6 KNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLpelcSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGEL--F--EDIVAREYYSEADASHCIQQILEAVLHCHQMG---VVHRDLKPENLLLASKCKGAAVKLADFGL 160
Cdd:cd05036  86 ILLELMAGGDLksFlrENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEenhFIHRDIAARNCLLTCKGPGRVAKIGDFGM 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 161 AIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPF 214
Cdd:cd05036 166 ARDIyRADYYRKGGKAMLPvKWMPPEAFLDGIFTSKTDVWSFGVLLWeIFSLGYMPY 222
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
119-229 1.17e-10

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: 61.90  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 119 QILEAVLHCHQMGVVHRDLKPENLLLAS--KCKGAAVKLADFGlaIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVD 196
Cdd:cd14067 122 QIAAGLAYLHKKNIIFCDLKSDNILVWSldVQEHINIKLSDYG--ISRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVD 199
                        90       100       110
                ....*....|....*....|....*....|...
gi 26051218 197 IWACGVILYILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd14067 200 MFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
DUF4440 pfam14534
Domain of unknown function (DUF4440);
321-434 1.19e-10

Domain of unknown function (DUF4440);


Pssm-ID: 434023 [Multi-domain]  Cd Length: 107  Bit Score: 58.18  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218   321 IIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPeaLGNLVEGMDFHRFYFENLLAKNSkpihTTILNPHVHVIGEDAACI 400
Cdd:pfam14534   1 IRALEEALLEALVAGDPAALAALLAPDFVLVGP--SGPVLDKDEILEALASGGLDYSS----IELEDEKVRVLGDTAVVR 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 26051218   401 AYIRLTqyIDGQGRPRTSQSEETRVWHRRDGKWQ 434
Cdd:pfam14534  75 GRVTVT--GRGDGEPVTVRGRFTSVWKKEGGGWK 106
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
109-271 1.24e-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: 61.95  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 109 SEADASHCIQQILEAV--LHCHQmGVVHRDLKPENLLLASKckGAAvKLADFGLAIEVQ--GDQQAWFGFAG-------- 176
Cdd:cd14011 112 YDVEIKYGLLQISEALsfLHNDV-KLVHGNICPESVVINSN--GEW-KLAGFDFCISSEqaTDQFPYFREYDpnlpplaq 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 -TPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLyqqikagAYDFPSPEWDTVTPEAKNLINQ---- 251
Cdd:cd14011 188 pNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLL-------SYKKNSNQLRQLSLSLLEKVPEelrd 260
                       170       180
                ....*....|....*....|....
gi 26051218 252 ----MLTINPAKRITAHEALKHPW 271
Cdd:cd14011 261 hvktLLNVTPEVRPDAEQLSKIPF 284
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
57-260 1.78e-10

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: 61.10  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  57 KLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFE-------DIVAREYYSEADASHCIQQILEAVlHChq 129
Cdd:cd05084  40 KFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTflrtegpRLKVKELIRMVENAAAGMEYLESK-HC-- 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 130 mgvVHRDLKPENLLLASKckgAAVKLADFGLAIEVQ-GDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-I 206
Cdd:cd05084 117 ---IHRDLAARNCLVTEK---NVLKISDFGMSREEEdGVYAATGGMKQIPvKWTAPEALNYGRYSSESDVWSFGILLWeT 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 207 LLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEwdTVTPEAKNLINQMLTINPAKR 260
Cdd:cd05084 191 FSLGAVPYANLSNQQTREAVEQG-VRLPCPE--NCPDEVYRLMEQCWEYDPRKR 241
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
15-214 2.33e-10

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). 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 Hck 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: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 60.81  E-value: 2.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGAFSVVRrcvkLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFDLVT 94
Cdd:cd05073  14 KLEKKLGAGQFGEVW----MATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPI-YIITEFMA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFeDIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGDQQAW 171
Cdd:cd05073  89 KGSLL-DFLKSDEGSKQPLPKLIDfsaQIAEGMAFIEQRNYIHRDLRAANILVS---ASLVCKIADFGLARVIEDNEYTA 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 26051218 172 FGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPF 214
Cdd:cd05073 165 REGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLMeIVTYGRIPY 209
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
40-213 2.88e-10

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: 60.88  E-value: 2.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  40 YAAKIINTK--KLSARDHQK-LEREARICRLLKHSNIV--RLHDSiSEEGFHYLVFDlvTGGELFEDIVAREYYSEADA- 113
Cdd:cd14001  31 WAVKKINSKcdKGQRSLYQErLKEEAKILKSLNHPNIVgfRAFTK-SEDGSLCLAME--YGGKSLNDLIEERYEAGLGPf 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 114 -SHCIQQILEAV------LHcHQMGVVHRDLKPENLLLASKCKgaAVKLADFGLAI----EVQGDQQAWFGFAGTPGYLS 182
Cdd:cd14001 108 pAATILKVALSIaraleyLH-NEKKILHGDIKSGNVLIKGDFE--SVKLCDFGVSLplteNLEVDSDPKAQYVGTEPWKA 184
                       170       180       190
                ....*....|....*....|....*....|....*
gi 26051218 183 PEVLRKeayGKPV----DIWACGVILYILLVGYPP 213
Cdd:cd14001 185 KEALEE---GGVItdkaDIFAYGLVLWEMMTLSVP 216
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
12-262 3.40e-10

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: 60.80  E-value: 3.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKI--INTKKL----SARDHQKLEREARICRLL-KHSNIVRLHDSISEEG 84
Cdd:cd05098  13 DRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVtkVAVKMLksdaTEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGGELFEDIVAR----------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskc 148
Cdd:cd05098  93 PLYVIVEYASKGNLREYLQARrppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT--- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 149 KGAAVKLADFGLAIEVQG-DQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQ 225
Cdd:cd05098 170 EDNVMKIADFGLARDIHHiDYYKKTTNGRLPvKWMAPEALFDRIYTHQSDVWSFGVLLWeIFTLGGSPYPGVPVEELFKL 249
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26051218 226 IKAG-AYDFPSpewdTVTPEAKNLINQMLTINPAKRIT 262
Cdd:cd05098 250 LKEGhRMDKPS----NCTNELYMMMRDCWHAVPSQRPT 283
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
20-214 3.49e-10

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 60.51  E-value: 3.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRR---CVKLCTGHEYAAKIINTKKLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05044   3 LGSGAFGEVFEgtaKDILGDGSGETKVAVKTLRKGATDQEKAEflKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELFEDI----VAREYYSEADASHCIQQILEAVLHCH---QMGVVHRDLKPENLLLASK-CKGAAVKLADFGLAIEV-Q 165
Cdd:cd05044  83 GGDLLSYLraarPTAFTPPLLTLKDLLSICVDVAKGCVyleDMHFVHRDLAARNCLVSSKdYRERVVKIGDFGLARDIyK 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26051218 166 GDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPF 214
Cdd:cd05044 163 NDYYRKEGEGLLPvRWMAPESLVDGVFTTQSDVWAFGVLMWeILTLGQQPY 213
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
19-208 3.92e-10

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: 60.33  E-value: 3.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVrrcvKLC--------TGHEYAAKiiNTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFH--Y 87
Cdd:cd05079  11 DLGEGHFGKV----ELCrydpegdnTGEQVAVK--SLKPESGGNHiADLKKEIEILRNLYHENIVKYKGICTEDGGNgiK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  88 LVFDLVTGGELfedivaREYYSEADASHCIQQILE-AVLHCHQMGV------VHRDLKPENLLLASKckgAAVKLADFGL 160
Cdd:cd05079  85 LIMEFLPSGSL------KEYLPRNKNKINLKQQLKyAVQICKGMDYlgsrqyVHRDLAARNVLVESE---HQVKIGDFGL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 161 AIEVQGDQQAW----------FGFAgtpgylsPEVLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd05079 156 TKAIETDKEYYtvkddldspvFWYA-------PECLIQSKFYIASDVWSFGVTLYELL 206
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-262 4.20e-10

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: 60.06  E-value: 4.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFhYLVFDLVTG 95
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEflREASVMAQLDHPCIVRLIGVCKGEPL-MLVMELAPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfgFA 175
Cdd:cd05060  80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR---HQAKISDFGMSRALGAGSDYY--RA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 176 GTPG-----YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPewDTVTPEAKNLI 249
Cdd:cd05060 155 TTAGrwplkWYAPECINYGKFSSKSDVWSYGVTLWeAFSYGAKPYGEMKGPEVIAMLESG-ERLPRP--EECPQEIYSIM 231
                       250
                ....*....|...
gi 26051218 250 NQMLTINPAKRIT 262
Cdd:cd05060 232 LSCWKYRPEDRPT 244
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
20-236 4.29e-10

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: 60.27  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVrrC---VKLCTGHEYAAKIiNTKKLSARDHQKLE--REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVT 94
Cdd:cd05066  12 IGAGEFGEV--CsgrLKLPGKREIPVAI-KTLKAGYTEKQRRDflSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  95 GGELfeDIVAREYyseaDASHCIQQ-------ILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGD 167
Cdd:cd05066  89 NGSL--DAFLRKH----DGQFTVIQlvgmlrgIASGMKYLSDMGYVHRDLAARNILVNSNL---VCKVSDFGLSRVLEDD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 168 QQAWFGFAGTP---GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSP 236
Cdd:cd05066 160 PEAAYTTRGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAIEEG-YRLPAP 231
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
20-205 5.32e-10

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: 59.98  E-value: 5.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcvklctGHeYAAKIINTKKLSARDHQKLEREARI--CRLLKHSNIVRLHDS-ISEEGFH---YLVFDLV 93
Cdd:cd14056   3 IGKGRYGEVWL------GK-YRGEKVAVKIFSSRDEDSWFRETEIyqTVMLRHENILGFIAAdIKSTGSWtqlWLITEYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFeDIVAREYYSEADASHCIQQILEAVLHCH--------QMGVVHRDLKPENLLlaskckgaaVK------LADFG 159
Cdd:cd14056  76 EHGSLY-DYLQRNTLDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNIL---------VKrdgtccIADLG 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 160 LAieVQGDQQAWFGFA------GTPGYLSPEVLRK-------EAYgKPVDIWACGVILY 205
Cdd:cd14056 146 LA--VRYDSDTNTIDIppnprvGTKRYMAPEVLDDsinpksfESF-KMADIYSFGLVLW 201
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
18-205 6.23e-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: 59.66  E-value: 6.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCVKLCTGHEY---AAKIINTKKLSARDH-QKLEREARICRLLKHSNIVRLHDSISEEGFHyLVFDLV 93
Cdd:cd05040   1 EKLGDGSFGVVRRGEWTTPSGKViqvAVKCLKSDVLSQPNAmDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLM-MVTELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDI--VAREYYSEADASHCIQqILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGL--AIEVQGD-- 167
Cdd:cd05040  80 PLGSLLDRLrkDQGHFLISTLCDYAVQ-IANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLmrALPQNEDhy 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 26051218 168 ---QQAWFGFAgtpgYLSPEVLRKEAYGKPVDIWACGVILY 205
Cdd:cd05040 156 vmqEHRKVPFA----WCAPESLKTRKFSHASDVWMFGVTLW 192
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
12-237 6.25e-10

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: 60.19  E-value: 6.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKlEREARICRLL------KHSNIVRLHDSISEEGF 85
Cdd:cd05055  35 NNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSS-EREALMSELKimshlgNHENIVNLLGACTIGGP 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGEL--FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKGAAVKLADFGLAIE 163
Cdd:cd05055 114 ILVITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL---THGKIVKICDFGLARD 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 164 VQGDQQAWF-GFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDED-QHKLYQQIKAGaYDFPSPE 237
Cdd:cd05055 191 IMNDSNYVVkGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWeIFSLGSNPYPGMPvDSKFYKLIKEG-YRMAQPE 267
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-272 6.28e-10

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: 60.14  E-value: 6.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTK-KLSARdhQKLEREARICRLLKHSNIVRL-----HD---SISE 82
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEiKPAIR--NQIIRELKVLHECNSPYIVGFygafySDgeiSICM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  83 EGFHYLVFDLV--TGGELFEDIVAReyyseadASHCIQQILEAVLHCHQmgVVHRDLKPENLLLASKckgAAVKLADFGl 160
Cdd:cd06615  79 EHMDGGSLDQVlkKAGRIPENILGK-------ISIAVLRGLTYLREKHK--IMHRDVKPSNILVNSR---GEIKLCDFG- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 aieVQG---DQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKL--------------- 222
Cdd:cd06615 146 ---VSGqliDSMA-NSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpvsegeake 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 223 -YQQIKAGAYDFPSP------------------EWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06615 222 sHRPVSGHPPDSPRPmaifelldyivnepppklPSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-234 6.95e-10

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: 60.07  E-value: 6.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06650   5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQII-RELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELfeDIVAREyyseadASHCIQQILEAVLHCHQMG---------VVHRDLKPENLLLASKckgAAVKLADFGLAI 162
Cdd:cd06650  84 HMDGGSL--DQVLKK------AGRIPEQILGKVSIAVIKGltylrekhkIMHRDVKPSNILVNSR---GEIKLCDFGVSG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26051218 163 EVQgDQQAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGY----PPFWDEDQHKLYQQIKAGAYDFP 234
Cdd:cd06650 153 QLI-DSMA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRypipPPDAKELELMFGCQVEGDAAETP 226
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
72-266 8.02e-10

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: 59.48  E-value: 8.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  72 NIVRLHDSISEEGFHYLVFDLVTGGELFEDIVarEYYSEADASH--------------------CIQQ----ILEAVLHC 127
Cdd:cd05576  52 NMVCLRKYIISEESVFLVLQHAEGGKLWSYLS--KFLNDKEIHQlfadlderlaaasrfyipeeCIQRwaaeMVVALDAL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 128 HQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVqgdQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYIL 207
Cdd:cd05576 130 HREGIVCRDLNPNNILLNDR---GHIQLTYFSRWSEV---EDSCDSDAIENMYCAPEVGGISEETEACDWWSLGALLFEL 203
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 208 LVGYPpfwdedqhkLYQQIKAGAYDFPS---PEWdtVTPEAKNLINQMLTINPAKRITAHEA 266
Cdd:cd05576 204 LTGKA---------LVECHPAGINTHTTlniPEW--VSEEARSLLQQLLQFNPTERLGAGVA 254
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
19-260 8.65e-10

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: 59.21  E-value: 8.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVVRRCV--KLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHdSISEEGFHYLVFDLVTGG 96
Cdd:cd05116   2 ELGSGNFGTVKKGYyqMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMI-GICEAESWMLVMEMAELG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWfgFAG 176
Cdd:cd05116  81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQ---HYAKISDFGLSKALRADENYY--KAQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 177 TPG-----YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGAyDFPSPEwdTVTPEAKNLIN 250
Cdd:cd05116 156 THGkwpvkWYAPECMNYYKFSSKSDVWSFGVLMWeAFSYGQKPYKGMKGNEVTQMIEKGE-RMECPA--GCPPEMYDLMK 232
                       250
                ....*....|
gi 26051218 251 QMLTINPAKR 260
Cdd:cd05116 233 LCWTYDVDER 242
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
15-216 9.52e-10

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: 59.38  E-value: 9.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGAFSVVRRcvKLCTGHEYAAKIintkkLSARDHQKLEREARICR--LLKHSNIVRL--HDSISEEGFH--YL 88
Cdd:cd14142   8 TLVECIGKGRYGEVWR--GQWQGESVAVKI-----FSSRDEKSWFRETEIYNtvLLRHENILGFiaSDMTSRNSCTqlWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  89 VFDLVTGGELFeDIVAREYYSEADASHCIQQILEAVLHCH--------QMGVVHRDLKPENLLLasKCKGAAVkLADFGL 160
Cdd:cd14142  81 ITHYHENGSLY-DYLQRTTLDHQEMLRLALSAASGLVHLHteifgtqgKPAIAHRDLKSKNILV--KSNGQCC-IADLGL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218 161 AI-EVQGDQQAWFGF---AGTPGYLSPEVLRK-------EAYgKPVDIWACGVILY----------ILLVGYPPFWD 216
Cdd:cd14142 157 AVtHSQETNQLDVGNnprVGTKRYMAPEVLDEtintdcfESY-KRVDIYAFGLVLWevarrcvsggIVEEYKPPFYD 232
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
12-272 1.07e-09

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: 59.31  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIIntkklsARDHQKlEREARICR-----LLKHS--NIVRLhdsiseeg 84
Cdd:cd06618  15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQM------RRSGNK-EENKRILMdldvvLKSHDcpYIVKC-------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDL------------------VTGGELFEDIVAREYYSEADASHCIQQileavlhchQMGVVHRDLKPENLLLAS 146
Cdd:cd06618  80 YGYFITDSdvficmelmstcldkllkRIQGPIPEDILGKMTVSIVKALHYLKE---------KHGVIHRDVKPSNILLDE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 147 KckgAAVKLADFGLAievqG---DQQAWFGFAGTPGYLSPEVL---RKEAYGKPVDIWACGVILYILLVGYPPFwDEDQH 220
Cdd:cd06618 151 S---GNVKLCDFGIS----GrlvDSKAKTRSAGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPY-RNCKT 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 26051218 221 KLYQQIKAGAYDFPSPEWD-TVTPEAKNLINQMLTINPAKRITAHEALKHPWV 272
Cdd:cd06618 223 EFEVLTKILNEEPPSLPPNeGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFI 275
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
60-269 1.12e-09

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 58.97  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  60 REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFeDIVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRD 136
Cdd:cd05052  51 KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLL-DYLRECNREELNAVvllYMATQIASAMEYLEKKNFIHRD 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 137 LKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPF 214
Cdd:cd05052 130 LAARNCLVGEN---HLVKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWeIATYGMSPY 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 215 WDEDQHKLYQQIKAGaYDFPSPEwdTVTPEAKNLINQMLTINPAKRIT---AHEALKH 269
Cdd:cd05052 207 PGIDLSQVYELLEKG-YRMERPE--GCPPKVYELMRACWQWNPSDRPSfaeIHQALET 261
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
12-229 1.14e-09

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: 59.26  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFS--VVRRCVKLCTGHEYAAKIINTKKL----SARDHQKLEREARICRLL-KHSNIVRLHDSISEEG 84
Cdd:cd05101  24 DKLTLGKPLGEGCFGqvVMAEAVGIDKDKPKEAVTVAVKMLkddaTEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  85 FHYLVFDLVTGGELFEDIVAR----------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskc 148
Cdd:cd05101 104 PLYVIVEYASKGNLREYLRARrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVT--- 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 149 KGAAVKLADFGLAIEVQG-DQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQ 225
Cdd:cd05101 181 ENNVMKIADFGLARDINNiDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLMWeIFTLGGSPYPGIPVEELFKL 260

                ....
gi 26051218 226 IKAG 229
Cdd:cd05101 261 LKEG 264
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
13-270 1.15e-09

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: 58.79  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14139   1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAR----EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLaskCKgaavKLADFGLAIEVQGD 167
Cdd:cd14139  81 YCNGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI---CH----KMQSSSGVGEEVSN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAWFGFA----------------------GTPGYLSPEVLRKEAYGKP-VDIWACGVILyILLVGYPPFwdEDQHKLYQ 224
Cdd:cd14139 154 EEDEFLSAnvvykigdlghvtsinkpqveeGDSRFLANEILQEDYRHLPkADIFALGLTV-ALAAGAEPL--PTNGAAWH 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 26051218 225 QIKAGayDFPS-PEwdTVTPEAKNLINQMLTINPAKRITAHEALKHP 270
Cdd:cd14139 231 HIRKG--NFPDvPQ--ELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
16-265 1.17e-09

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: 58.73  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  16 LYEDIGKGAFSVVRRCVKLctGHEYAAKIINTKKLSardhQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFDLVTG 95
Cdd:cd05083  10 LGEIIGEGEFGAVLQGEYM--GQKVAVKNIKCDVTA----QAFLEETAVMTKLQHKNLVRLLGVILHNGL-YIVMELMSK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GEL--FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckGAAvKLADFGLA-IEVQGDQQAWF 172
Cdd:cd05083  83 GNLvnFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSED--GVA-KISDFGLAkVGSMGVDNSRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 173 GFAGTpgylSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPEwdTVTPEAKNLINQ 251
Cdd:cd05083 160 PVKWT----APEALKNKKFSSKSDVWSYGVLLWeVFSYGRAPYPKMSVKEVKEAVEKG-YRMEPPE--GCPPDVYSIMTS 232
                       250
                ....*....|....
gi 26051218 252 MLTINPAKRITAHE 265
Cdd:cd05083 233 CWEAEPGKRPSFKK 246
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
15-260 1.25e-09

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. 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 Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 58.87  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGAFSvvrrcvKLCTGHEY-----AAKIINTKKL----SARDHQKLEREARICRLLKHSNIVRLHDSISEEGF 85
Cdd:cd05090   8 RFMEELGECAFG------KIYKGHLYlpgmdHAQLVAIKTLkdynNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  86 HYLVFDLVTGGELFEDIVAREYYSEADAS-----------------HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKC 148
Cdd:cd05090  82 VCMLFEFMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 149 KgaaVKLADFGLAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQ 225
Cdd:cd05090 162 H---VKISDLGLSREIySSDYYRVQNKSLLPiRWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEM 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 26051218 226 IKAGAYdFPSPEwdTVTPEAKNLINQMLTINPAKR 260
Cdd:cd05090 239 VRKRQL-LPCSE--DCPPRMYSLMTECWQEIPSRR 270
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
20-214 1.47e-09

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: 58.17  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcvklctGHEY---AAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHyLVFDLVTGG 96
Cdd:cd14062   1 IGSGSFGTVYK------GRWHgdvAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLA-IVTQWCEGS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREyySEADASHCI---QQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVKLADFGLAI------EVQGD 167
Cdd:cd14062  74 SLYKHLHVLE--TKFEMLQLIdiaRQTAQGMDYLHAKNIIHRDLKSNNIFLHE---DLTVKIGDFGLATvktrwsGSQQF 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 26051218 168 QQAwfgfAGTPGYLSPEVLR---KEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14062 149 EQP----TGSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQLPY 194
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-214 1.56e-09

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: 58.53  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRRCvklcTGH-EYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVrLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14151  14 QRIGSGSFGTVYKG----KWHgDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAREYYSEADASHCI-QQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAIEvqgdQQAWFG-- 173
Cdd:cd14151  89 SLYHHLHIIETKFEMIKLIDIaRQTAQGMDYLHAKSIIHRDLKSNNIFLH---EDLTVKIGDFGLATV----KSRWSGsh 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 174 ----FAGTPGYLSPEVLR---KEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14151 162 qfeqLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
20-208 1.69e-09

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: 58.58  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGH----EYAAKIINTKKlSARDHQKLEREARICRLLKHSNIVRLHdSISEEGFHYLVFDLVTG 95
Cdd:cd05057  15 LGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREET-GPKANEEILDEAYVMASVDHPHLVRLL-GICLSSQVQLITQLMPL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIvaREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAWF 172
Cdd:cd05057  93 GCLLDYV--RNHRDNIGSQLLLNwcvQIAKGMSYLEEKRLVHRDLAARNVLVKTP---NHVKITDFGLAKLLDVDEKEYH 167
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 26051218 173 GFAG-TP-GYLSPEVLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd05057 168 AEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELM 205
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-246 2.11e-09

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: 58.52  E-value: 2.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLeREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd06649   5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQII-RELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEDIVAREYYSE---ADASHCIQQILEAVLHCHQmgVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQgDQ 168
Cdd:cd06649  84 HMDGGSLDQVLKEAKRIPEeilGKVSIAVLRGLAYLREKHQ--IMHRDVKPSNILVNSR---GEIKLCDFGVSGQLI-DS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 169 QAwFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAK 246
Cdd:cd06649 158 MA-NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPR 234
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
45-262 2.18e-09

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: 58.19  E-value: 2.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  45 INTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEdivareyYSEADASHC-------- 116
Cdd:cd05068  37 VKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLE-------YLQGKGRSLqlpqlidm 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLA--IEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKP 194
Cdd:cd05068 110 AAQVASGMAYLESQNYIHRDLAARNVLVG---ENNICKVADFGLArvIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIK 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26051218 195 VDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPewDTVTPEAKNLINQMLTINPAKRIT 262
Cdd:cd05068 187 SDVWSFGILLTeIVTYGRIPYPGMTNAEVLQQVERG-YRMPCP--PNCPPQLYDIMLECWKADPMERPT 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
20-260 2.21e-09

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: 58.13  E-value: 2.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSAR-DHQKLEREARI-CRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGE 97
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKdDHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LFeDIVAREYYSEADASHCI----------QQILE-------AVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGL 160
Cdd:cd05047  83 LL-DFLRKSRVLETDPAFAIanstastlssQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVG---ENYVAKIADFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 161 AievQGDQqawFGFAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFP 234
Cdd:cd05047 159 S---RGQE---VYVKKTMGrlpvrWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG-YRLE 231
                       250       260
                ....*....|....*....|....*.
gi 26051218 235 SPEwdTVTPEAKNLINQMLTINPAKR 260
Cdd:cd05047 232 KPL--NCDDEVYDLMRQCWREKPYER 255
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
45-236 2.30e-09

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing 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 with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src 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: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 58.16  E-value: 2.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  45 INTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFDLVTGGELFEDIVAR--EYYSEADASHCIQQILE 122
Cdd:cd05071  38 IKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPI-YIVTEYMSKGSLLDFLKGEmgKYLRLPQLVDMAAQIAS 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 123 AVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAIEVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACG 201
Cdd:cd05071 117 GMAYVERMNYVHRDLRAANILVGENL---VCKVADFGLARLIEDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFG 193
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 26051218 202 VILYILLV-GYPPFWDEDQHKLYQQIKAGaYDFPSP 236
Cdd:cd05071 194 ILLTELTTkGRVPYPGMVNREVLDQVERG-YRMPCP 228
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
20-236 2.49e-09

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 58.01  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAF-SVVRRCVKLCTGHEYAAKIiNTKKLSARDHQKLEREARICRL--LKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd05064  13 LGTGRFgELCRGCLKLPSKRELPVAI-HTLRAGCSDKQRRGFLAEALTLgqFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELfeDIVAREYYSEADASHC---IQQILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGlaiEVQGDQ-QAWF 172
Cdd:cd05064  92 AL--DSFLRKHEGQLVAGQLmgmLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDL---VCKISGFR---RLQEDKsEAIY 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 173 GFAGTPG---YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSP 236
Cdd:cd05064 164 TTMSGKSpvlWAAPEAIQYHHFSSASDVWSFGIVMWeVMSYGERPYWDMSGQDVIKAVEDG-FRLPAP 230
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
39-271 2.68e-09

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: 58.16  E-value: 2.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  39 EYAAKIINTKKLSardhQKLEREARICRLLKHSNIVRLHDSISEEGFH--YLVFDLVTGgELFEdIVAREYYSEAD---- 112
Cdd:cd07867  31 EYALKQIEGTGIS----MSACREIALLRELKHPNVIALQKVFLSHSDRkvWLLFDYAEH-DLWH-IIKFHRASKANkkpm 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 113 ------ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKC-KGAAVKLADFGLAIEVQGDQQAWFGF---AGTPGYLS 182
Cdd:cd07867 105 qlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRA 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 183 PEVLR-KEAYGKPVDIWACGVILYILLVGYPPFW--DED-------QHKLYQQIKAgAYDFPS----------PEWDT-- 240
Cdd:cd07867 185 PELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHcrQEDiktsnpfHHDQLDRIFS-VMGFPAdkdwedirkmPEYPTlq 263
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 241 ---------------------VTPEAKN--LINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07867 264 kdfrrttyansslikymekhkVKPDSKVflLLQKLLTMDPTKRITSEQALQDPY 317
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
53-229 3.08e-09

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: 58.11  E-value: 3.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  53 RDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAR----------------EYYSEADASH 115
Cdd:cd05100  59 KDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARrppgmdysfdtcklpeEQLTFKDLVS 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 116 CIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQG-DQQAWFGFAGTP-GYLSPEVLRKEAYGK 193
Cdd:cd05100 139 CAYQVARGMEYLASQKCIHRDLAARNVLVTED---NVMKIADFGLARDVHNiDYYKKTTNGRLPvKWMAPEALFDRVYTH 215
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26051218 194 PVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05100 216 QSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKEG 252
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
51-229 3.31e-09

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: 58.05  E-value: 3.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  51 SARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAR----------------EYYSEADA 113
Cdd:cd05099  57 TDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdytfditkvpeEQLSFKDL 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 114 SHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAievQGDQQAWFGFAGTPG-----YLSPEVLRK 188
Cdd:cd05099 137 VSCAYQVARGMEYLESRRCIHRDLAARNVLVTED---NVMKIADFGLA---RGVHDIDYYKKTSNGrlpvkWMAPEALFD 210
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 26051218 189 EAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05099 211 RVYTHQSDVWSFGILMWeIFTLGGSPYPGIPVEELFKLLREG 252
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
14-214 3.87e-09

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: 57.37  E-value: 3.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQKLEREARICRLLK-HSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14129   2 WKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQ----PKQVLKMEVAVLKKLQgKDHVCRFIGCGRNDRFNYVVMQL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 vtGGELFEDI---VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA---SKCKgaAVKLADFGLAIEVQ- 165
Cdd:cd14129  78 --QGRNLADLrrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCR--KCYMLDFGLARQFTn 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 166 --GD---QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14129 154 scGDvrpPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 207
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
35-281 3.95e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 57.69  E-value: 3.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  35 CTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELfEDIVaREYYSEADAS 114
Cdd:cd08216  23 PTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSC-RDLL-KTHFPEGLPE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 115 HCIQQILEAVLHC----HQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIE-VQGDQQAWFGFAGTPG------YLSP 183
Cdd:cd08216 101 LAIAFILRDVLNAleyiHSKGYIHRSVKASHILISGDGK---VVLSGLRYAYSmVKHGKRQRVVHDFPKSseknlpWLSP 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 184 EVLRK--EAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLY-QQIKAGAYD------FPSPEWD--------------- 239
Cdd:cd08216 178 EVLQQnlLGYNEKSDIYSVGITACELANGVVPFSDMPATQMLlEKVRGTTPQlldcstYPLEEDSmsqsedsstehpnnr 257
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 240 ---------TVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ-RSTVASM 281
Cdd:cd08216 258 dtrdipyqrTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQcRRSNTSL 309
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-214 4.06e-09

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: 57.35  E-value: 4.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCvklcTGH-EYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHyLVF 90
Cdd:cd14149  12 SEVMLSTRIGSGSFGTVYKG----KWHgDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDI-VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLAI---EVQG 166
Cdd:cd14149  87 QWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKIGDFGLATvksRWSG 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26051218 167 DQQAWfGFAGTPGYLSPEVLRKE---AYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14149 164 SQQVE-QPTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPY 213
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
132-274 5.97e-09

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: 56.81  E-value: 5.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 132 VVHRDLKPENLLLASKckgAAVKLADFGLAIEVQGDQQAwfGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVG- 210
Cdd:cd06619 116 ILHRDVKPSNMLVNTR---GQVKLCDFGVSTQLVNSIAK--TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGr 190
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 211 --YPPFWDEDQHKLYQQIKAGAYDFPSPEWDT--VTPEAKNLINQMLTINPAKRITAHEALKHPWVCQ 274
Cdd:cd06619 191 fpYPQIQKNQGSLMPLQLLQCIVDEDPPVLPVgqFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQ 258
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
12-262 6.00e-09

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. 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 Lck/Blk 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: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 56.82  E-value: 6.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVrrCVKLCTGHEYAAkiINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFhYLVFD 91
Cdd:cd05067   7 ETLKLVERLGAGQFGEV--WMGYYNGHTKVA--IKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPI-YIITE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEdivareyYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLAI 162
Cdd:cd05067  82 YMENGSLVD-------FLKTPSGIKLTinklldmaaQIAEGMAFIEERNYIHRDLRAANILVSDTL---SCKIADFGLAR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 163 EVQGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPewDT 240
Cdd:cd05067 152 LIEDNEYTAREGAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTeIVTHGRIPYPGMTNPEVIQNLERG-YRMPRP--DN 228
                       250       260
                ....*....|....*....|..
gi 26051218 241 VTPEAKNLINQMLTINPAKRIT 262
Cdd:cd05067 229 CPEELYQLMRLCWKERPEDRPT 250
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
13-229 7.11e-09

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: 56.43  E-value: 7.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCvKLCTGHEYAAKIINTKKLSARDhqkLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05113   5 DLTFLKELGTGQFGVVKYG-KWRGQYDVAIKMIKEGSMSEDE---FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEdivareYYSEADASHCIQQILE---------AVLHCHQMgvVHRDLKPENLLLASKckgAAVKLADFGLAIE 163
Cdd:cd05113  81 MANGCLLN------YLREMRKRFQTQQLLEmckdvceamEYLESKQF--LHRDLAARNCLVNDQ---GVVKVSDFGLSRY 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 164 VQGDQQAWFGFAGTPGYLS-PEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05113 150 VLDDEYTSSVGSKFPVRWSpPEVLMYSKFSSKSDVWAFGVLMWeVYSLGKMPYERFTNSETVEHVSQG 217
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
16-229 8.16e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) 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 of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 56.59  E-value: 8.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  16 LYEDIGKGAFSVV--RRCVKLCTGHEYAAKIINT-KKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDL 92
Cdd:cd05093   9 LKRELGEGAFGKVflAECYNLCPEQDKILVAVKTlKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 VTGGELFEDIVAR-------------EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFG 159
Cdd:cd05093  89 MKHGDLNKFLRAHgpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG---ENLLVKIGDFG 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26051218 160 LAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05093 166 MSRDVySTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 238
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
37-271 9.19e-09

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: 56.60  E-value: 9.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  37 GHEYAAKIINTKKLSARDHQKLE---------REARICRLLKHSNIVRLHDSISEEGFH--YLVFDLVTGgELFEdIVAR 105
Cdd:cd07868  31 GHVYKAKRKDGKDDKDYALKQIEgtgismsacREIALLRELKHPNVISLQKVFLSHADRkvWLLFDYAEH-DLWH-IIKF 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 106 EYYSEAD----------ASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKC-KGAAVKLADFGLAIEVQGDQQAWFGF 174
Cdd:cd07868 109 HRASKANkkpvqlprgmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLFNSPLKPLADL 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 175 ---AGTPGYLSPEVLR-KEAYGKPVDIWACGVILYILLVGYPPF--------------------------------WDE- 217
Cdd:cd07868 189 dpvVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktsnpyhhdqldrifnvmgfpadkdWEDi 268
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 218 ----DQHKLYQQIKAGAYDFPS----PEWDTVTPEAK--NLINQMLTINPAKRITAHEALKHPW 271
Cdd:cd07868 269 kkmpEHSTLMKDFRRNTYTNCSlikyMEKHKVKPDSKafHLLQKLLTMDPIKRITSEQAMQDPY 332
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
19-215 1.18e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) 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 of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 56.13  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVV--RRCVKLCTGHE---YAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd05092  12 ELGEGAFGKVflAECHNLLPEQDkmlVAVKALKEATESAR--QDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAR------------EYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADF 158
Cdd:cd05092  90 RHGDLNRFLRSHgpdakildggegQAPGQLTLGQMLQiasQIASGMVYLASLHFVHRDLATRNCLVG---QGLVVKIGDF 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 159 GLAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFW 215
Cdd:cd05092 167 GMSRDIySTDYYRVGGRTMLPiRWMPPESILYRKFTTESDIWSFGVVLWeIFTYGKQPWY 226
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
43-208 1.29e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 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 catalytic 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 Tyk2 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: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 55.68  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  43 KIINTKKLSARDHQKLE----REARICRLLKHSNIVRLHDSISEEGFH--YLVFDLVTGGELfEDIVAREYYSEADASHC 116
Cdd:cd05080  34 EMVAVKALKADCGPQHRsgwkQEIDILKTLYHENIVKYKGCCSEQGGKslQLIMEYVPLGSL-RDYLPKHSIGLAQLLLF 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 117 IQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEV-----------QGDQQA-WFgfagtpgylSPE 184
Cdd:cd05080 113 AQQICEGMAYLHSQHYIHRDLAARNVLLDND---RLVKIGDFGLAKAVpegheyyrvreDGDSPVfWY---------APE 180
                       170       180
                ....*....|....*....|....
gi 26051218 185 VLRKEAYGKPVDIWACGVILYILL 208
Cdd:cd05080 181 CLKEYKFYYASDVWSFGVTLYELL 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
15-210 1.38e-08

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: 55.57  E-value: 1.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklSARDHQKLEREARICRLL-KHSNIVRLHDSISEEGFhylvfdlv 93
Cdd:cd13975   3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVVPP--DDKHWNDLALEFHYTRSLpKHERIVSLHGSVIDYSY-------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGE-----LFEDIVAREYYSEADASHCIQQ-------ILEAVLHCHQMGVVHRDLKPENLLLASKCKGaavKLADFGLA 161
Cdd:cd13975  73 GGGSsiavlLIMERLHRDLYTGIKAGLSLEErlqialdVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA---KITDLGFC 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 162 IE---VQGDqqawfgFAGTPGYLSPEVLRKEaYGKPVDIWACGVILYILLVG 210
Cdd:cd13975 150 KPeamMSGS------IVGTPIHMAPELFSGK-YDNSVDVYAFGILFWYLCAG 194
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
20-205 1.43e-08

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: 55.85  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRcVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRL--LKHSNIVRLHDSISEEGFHYLVFDLVTG-- 95
Cdd:cd14055   3 VGKGRFAEVWK-AKLKQNASGQYETVAVKIFPYEEYASWKNEKDIFTDasLKHENILQFLTAEERGVGLDRQYWLITAyh 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 --GELfEDIVAREYYSEADASHCIQQILEAVLHCH---------QMGVVHRDLKPENLLLasKCKGAAVkLADFGLAIE- 163
Cdd:cd14055  82 enGSL-QDYLTRHILSWEDLCKMAGSLARGLAHLHsdrtpcgrpKIPIAHRDLKSSNILV--KNDGTCV-LADFGLALRl 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26051218 164 ---VQGDQQAWFGFAGTPGYLSPEVLRK-------EAYgKPVDIWACGVILY 205
Cdd:cd14055 158 dpsLSVDELANSGQVGTARYMAPEALESrvnledlESF-KQIDVYSMALVLW 208
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
17-229 1.47e-08

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: 55.78  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YED-IGKGAFSVVRRCVKLCTGHEYAAKIINTKKL-SARDHQKLEREARI-CRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd05089   6 FEDvIGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFaSENDHRDFAGELEVlCKLGHHPNIINLLGACENRGYLYIAIEYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELF-----------EDIVAREYYSEADASHciQQILE-------AVLHCHQMGVVHRDLKPENLLLAskcKGAAVKL 155
Cdd:cd05089  86 PYGNLLdflrksrvletDPAFAKEHGTASTLTS--QQLLQfasdvakGMQYLSEKQFIHRDLAARNVLVG---ENLVSKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 156 ADFGLAievQGDQqawFGFAGTPG-----YLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05089 161 ADFGLS---RGEE---VYVKKTMGrlpvrWMAIESLNYSVYTTKSDVWSFGVLLWeIVSLGGTPYCGMTCAELYEKLPQG 234
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
60-237 1.49e-08

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: 55.37  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  60 REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEdivareyYSEADASHCIQ---------QILEAVLHCHQM 130
Cdd:cd05034  39 QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD-------YLRTGEGRALRlpqlidmaaQIASGMAYLESR 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 131 GVVHRDLKPENLLLAskcKGAAVKLADFGLAIEVQGD-----QQAWFGFAGTpgylSPEVLRKEAYGKPVDIWACGVILY 205
Cdd:cd05034 112 NYIHRDLAARNILVG---ENNVCKVADFGLARLIEDDeytarEGAKFPIKWT----APEAALYGRFTIKSDVWSFGILLY 184
                       170       180       190
                ....*....|....*....|....*....|...
gi 26051218 206 -ILLVGYPPFWDEDQHKLYQQIKAGaYDFPSPE 237
Cdd:cd05034 185 eIVTYGRVPYPGMTNREVLEQVERG-YRMPKPP 216
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
36-243 1.54e-08

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 56.03  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  36 TGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEdiVAREYYSEADASH 115
Cdd:cd08226  24 TGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARG--LLKTYFPEGMNEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 116 CIQQILEAVL----HCHQMGVVHRDLKPENLLLASKckgAAVKLADF-GLAIEVQGDQQAWFGF------AGTPGYLSPE 184
Cdd:cd08226 102 LIGNILYGAIkalnYLHQNGCIHRSVKASHILISGD---GLVSLSGLsHLYSMVTNGQRSKVVYdfpqfsTSVLPWLSPE 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 185 VLRKEAYGKPV--DIWACGVILYILLVGYPPFWDEDQHK-LYQQIKAGAYdfpSPeWDTVTP 243
Cdd:cd08226 179 LLRQDLHGYNVksDIYSVGITACELARGQVPFQDMRRTQmLLQKLKGPPY---SP-LDIFPF 236
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
40-208 1.87e-08

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: 55.41  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  40 YAAKIINTKKLSARDHQKLEREARICRL--LKHSNIVRLHDS-------------ISEegFH-------YLVFDLVTGGE 97
Cdd:cd14053  16 YLNRLVAVKIFPLQEKQSWLTEREIYSLpgMKHENILQFIGAekhgesleaeywlITE--FHergslcdYLKGNVISWNE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  98 LF---EDIVAREYYSEADASHCIQQileavlhcHQMGVVHRDLKPENLLLASK---CkgaavkLADFGLAI-----EVQG 166
Cdd:cd14053  94 LCkiaESMARGLAYLHEDIPATNGG--------HKPSIAHRDFKSKNVLLKSDltaC------IADFGLALkfepgKSCG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 167 DQQawfGFAGTPGYLSPEVL------RKEAYgKPVDIWACGVILYILL 208
Cdd:cd14053 160 DTH---GQVGTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELL 203
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
17-217 1.88e-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: 55.19  E-value: 1.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  17 YEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGfhYLVFDLVTGG 96
Cdd:cd14025   1 WEKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPV--GLVMEYMETG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELfEDIVAREYYSEADASHCIQQILEAV--LHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEVQG---DQQAW 171
Cdd:cd14025  79 SL-EKLLASEPLPWELRFRIIHETAVGMnfLHCMKPPLLHLDLKPANILLDAHYH---VKISDFGLAKWNGLshsHDLSR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26051218 172 FGFAGTPGYLSPEVLRK--EAYGKPVDIWACGVILYILLVGYPPFWDE 217
Cdd:cd14025 155 DGLRGTIAYLPPERFKEknRCPDTKHDVYSFAIVIWGILTQKKPFAGE 202
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
14-161 1.91e-08

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon 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: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 55.07  E-value: 1.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQKLEREARICRLLKHS-NIVRLHDSISEEGFHYLVFDL 92
Cdd:cd14125   2 YRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKT----KHPQLLYESKLYKILQGGvGIPNVRWYGVEGDYNVMVMDL 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26051218  93 VtgGELFEDI---VAREYYSE-----ADashciqQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA 161
Cdd:cd14125  78 L--GPSLEDLfnfCSRKFSLKtvlmlAD------QMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLA 146
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
19-215 2.08e-08

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: 55.22  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  19 DIGKGAFSVV--RRCVKLCTGHEY---AAKIINtKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLV 93
Cdd:cd05050  12 DIGQGAFGRVfqARAPGLLPYEPFtmvAVKMLK-EEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  94 TGGELFEDIVAREYYSEADASH---------------------CI-QQILEAVLHCHQMGVVHRDLKPENLLLAskcKGA 151
Cdd:cd05050  91 AYGDLNEFLRHRSPRAQCSLSHstssarkcglnplplscteqlCIaKQVAAGMAYLSERKFVHRDLATRNCLVG---ENM 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26051218 152 AVKLADFGLAIEV------QGDQQAWFGFAGTPgylsPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFW 215
Cdd:cd05050 168 VVKIADFGLSRNIysadyyKASENDAIPIRWMP----PESIFYNRYTTESDVWAYGVVLWeIFSYGMQPYY 234
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
20-204 2.20e-08

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: 54.96  E-value: 2.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSvvrRCVKLCtgHEYAAKIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14221   1 LGKGCFG---QAIKVT--HRETGEVMVMKELIRFDEETQRtflKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVARE-YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLAskcKGAAVKLADFGLA-------------- 161
Cdd:cd14221  76 TLRGIIKSMDsHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVR---ENKSVVVADFGLArlmvdektqpeglr 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 26051218 162 IEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14221 153 SLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
15-260 2.80e-08

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 54.97  E-value: 2.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGAFSVVRRC----VKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05045   3 VLGKTLGEGEFGKVVKAtafrLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGEL---------------FEDIVAREYYSEADASHCIQ---------QILEAVLHCHQMGVVHRDLKPENLLLAs 146
Cdd:cd05045  83 EYAKYGSLrsflresrkvgpsylGSDGNRNSSYLDNPDERALTmgdlisfawQISRGMQYLAEMKLVHRDLAARNVLVA- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 147 kcKGAAVKLADFGLAIEVQGDQQAWFGFAG-TP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLY 223
Cdd:cd05045 162 --EGRKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIAPERLF 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 26051218 224 QQIKAGaYDFPSPEwdTVTPEAKNLINQMLTINPAKR 260
Cdd:cd05045 240 NLLKTG-YRMERPE--NCSEEMYNLMLTCWKQEPDKR 273
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
20-298 3.53e-08

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; 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. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 54.83  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVKLCTghEYAAKII--------NTKKLSARDH-QKLERearicrlLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLkedseldwSVVKNSFLTEvEKLSR-------FRHPNIVDLAGYSAQQGNYCLIY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELfEDIVAREYYSEA-----------DASHCIQqileaVLHCHQMGVVHRDLKPENLLLaskckGAAV--KLAD 157
Cdd:cd14159  72 VYLPNGSL-EDRLHCQVSCPClswsqrlhvllGTARAIQ-----YLHSDSPSLIHGDVKSSNILL-----DAALnpKLGD 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 158 FGLA----IEVQGDQQAWFG----FAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQ---I 226
Cdd:cd14159 141 FGLArfsrRPKQPGMSSTLArtqtVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKYLkdlV 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218 227 KAGAYDFPSPEWDTVTPEAKnlinqmlTINPAKRITAHEALKHPWVCQRStvASMMHRQETVECLKKFNARR 298
Cdd:cd14159 221 KEEEEAQHTPTTMTHSAEAQ-------AAQLATSICQKHLDPQAGPCPPE--LGIEISQLACRCLHRRAKKR 283
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
60-237 3.66e-08

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 53.88  E-value: 3.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  60 REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELfEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKP 139
Cdd:cd13973  50 RAARRLARLNDPGLARVLDAVAYRGGVYVVAEWVPGSSL-ADVAESGPLDPEAAARAVAELAEALAAAHRAGLALGIDHP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 140 ENLLLASkckGAAVKLAdfGLAIEVQGDQQAwfgfagtpgylspevlrkeaygkpvDIWACGVILYILLVGYPPFwDEDQ 219
Cdd:cd13973 129 DRVRISS---DGRVVLA--FPAVLAALSPAT-------------------------DVRALGALLYALLTGRWPL-PEGG 177
                       170
                ....*....|....*...
gi 26051218 220 HKLYQQIkAGAYDFPSPE 237
Cdd:cd13973 178 AALAAAP-ADAAEPVPPR 194
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
20-204 4.92e-08

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: 54.05  E-value: 4.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  20 IGKGAFSVVRRCVklctgHEYAAKIINTKKLSARDHQKLE---REARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGG 96
Cdd:cd14154   1 LGKGFFGQAIKVT-----HRETGEVMVMKELIRFDEEAQRnflKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  97 ELFEDIVAR-EYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKckgAAVKLADFGLAIEVQG--------- 166
Cdd:cd14154  76 TLKDVLKDMaRPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVRED---KTVVVADFGLARLIVEerlpsgnms 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 26051218 167 -----------DQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVIL 204
Cdd:cd14154 153 psetlrhlkspDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
119-229 1.17e-07

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: 52.84  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 119 QILEAVLHCHQMGVVHRDLKPENLLLASKCKgaaVKLADFGLAIEV-------QGDQQ----AWfgfagtpgyLSPEVLR 187
Cdd:cd05043 124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQ---VKITDNALSRDLfpmdyhcLGDNEnrpiKW---------MSLESLV 191
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 26051218 188 KEAYGKPVDIWACGVILYILL-VGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05043 192 NKEYSSASDVWSFGVLLWELMtLGQTPYVEIDPFEMAAYLKDG 234
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
18-265 1.48e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 52.68  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  18 EDIGKGAFSVVRrCVKLCTGHEYAAKIINTKKLSA--RDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTG 95
Cdd:cd05087   3 KEIGHGWFGKVF-LGEVNSGLSSTQVVVKELKASAsvQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  96 GELFEDIVA-REYYSEADASHCIQQ----ILEAVLHCHQMGVVHRDLKPENLLLASKCkgaAVKLADFGLA-------IE 163
Cdd:cd05087  82 GDLKGYLRScRAAESMAPDPLTLQRmaceVACGLLHLHRNNFVHSDLALRNCLLTADL---TVKIGDYGLShckykedYF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 164 VQGDQQaWFGFAgtpgYLSPEVLrKEAYG--------KPVDIWACGVILYILL-VGYPPFWD-EDQHKLYQQIKAGAYDF 233
Cdd:cd05087 159 VTADQL-WVPLR----WIAPELV-DEVHGnllvvdqtKQSNVWSLGVTIWELFeLGNQPYRHySDRQVLTYTVREQQLKL 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 26051218 234 PSPEWDTVTPEAKNLINQMLTINPAKRITAHE 265
Cdd:cd05087 233 PKPQLKLSLAERWYEVMQFCWLQPEQRPTAEE 264
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
14-214 1.58e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 52.34  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  14 YQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKlsarDHQKLEREARICRLLKHSN-IVRLHDSISEEGFHYLVFDL 92
Cdd:cd14130   2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ----PKQVLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  93 vtGGELFEDI---VAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLL---LASKCKgaAVKLADFGLA---IE 163
Cdd:cd14130  78 --QGRNLADLrrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYR--KCYMLDFGLArqyTN 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26051218 164 VQGD---QQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPF 214
Cdd:cd14130 154 TTGEvrpPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 207
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
16-215 2.42e-07

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) 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 of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 51.94  E-value: 2.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  16 LYEDIGKGAFSVV--RRCVKLCTGHE---YAAKIINTKKLSARdhQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF 90
Cdd:cd05094   9 LKRELGEGAFGKVflAECYNLSPTKDkmlVAVKTLKDPTLAAR--KDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  91 DLVTGGELFEDIVA-------------REYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckGAAVK 154
Cdd:cd05094  87 EYMKHGDLNKFLRAhgpdamilvdgqpRQAKGELGLSqmlHIATQIASGMVYLASQHFVHRDLATRNCLVGA---NLLVK 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 155 LADFGLAIEV-QGDQQAWFGFAGTP-GYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFW 215
Cdd:cd05094 164 IGDFGMSRDVySTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSFGVILWeIFTYGKQPWF 227
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
13-161 2.69e-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: 51.74  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  13 EYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKklsARdHQKLEREARICRLLKHS-NIVRLHDSISEEGFHYLVFD 91
Cdd:cd14128   1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQK---AR-HPQLLYESKLYKILQGGvGIPHIRWYGQEKDYNVLVMD 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26051218  92 LVtgGELFEDIV--AREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLA 161
Cdd:cd14128  77 LL--GPSLEDLFnfCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLA 146
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
12-229 2.95e-07

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: 51.92  E-value: 2.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  12 DEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARD-HQKLEREARI-CRLLKHSNIVRLHDSISEEGFHYLV 89
Cdd:cd05088   7 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDdHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  90 FDLVTGGELFeDIVAREYYSEADASHCI----------QQIL-------EAVLHCHQMGVVHRDLKPENLLLAskcKGAA 152
Cdd:cd05088  87 IEYAPHGNLL-DFLRKSRVLETDPAFAIanstastlssQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVG---ENYV 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26051218 153 VKLADFGLAIEVQGDQQAWFGFAGTPgYLSPEVLRKEAYGKPVDIWACGVILY-ILLVGYPPFWDEDQHKLYQQIKAG 229
Cdd:cd05088 163 AKIADFGLSRGQEVYVKKTMGRLPVR-WMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQG 239
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
15-297 3.41e-07

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: 51.51  E-value: 3.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  15 QLYEDIGKGafsvvrRCVKLCTGHEYAAKIINTKKLSA--RDHQKL-EREARICRLLKHSNIVRLHDSISEEGFHYLVFD 91
Cdd:cd14152   3 ELGELIGQG------RWGKVHRGRWHGEVAIRLLEIDGnnQDHLKLfKKEVMNYRQTRHENVVLFMGACMHPPHLAIITS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218  92 LVTGGELFEdiVAREYYSEADAS---HCIQQILEAVLHCHQMGVVHRDLKPENLLLASkckgAAVKLADFGLaievqgdq 168
Cdd:cd14152  77 FCKGRTLYS--FVRDPKTSLDINktrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGL-------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26051218 169 qawFGFAGTPG----------------YLSPEVLRKEAYG---------KPVDIWACGVILYILLVGYPPFWDEDQHKLY 223
Cdd:cd14152 143 ---FGISGVVQegrrenelklphdwlcYLAPEIVREMTPGkdedclpfsKAADVYAFGTIWYELQARDWPLKNQPAEALI 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26051218 224 QQIKAGaydfpspewdtvtpeaKNLINQMLTINPAKRITahEALKHPWVCQRSTVASMMHRQETVECLKKFNAR 297
Cdd:cd14152 220 WQIGSG----------------EGMKQVLTTISLGKEVT--EILSACWAFDLEERPSFTLLMDMLEKLPKLNRR 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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