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Conserved domains on  [gi|375493532|ref|NP_001243614|]
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maternal embryonic leucine zipper kinase isoform 2 [Homo sapiens]

Protein Classification

maternal embryonic leucine zipper kinase( domain architecture ID 10197385)

maternal embryonic leucine zipper kinase (MELK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
7-263 0e+00

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: 575.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14078    1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd14078   81 EYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd14078  161 TCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQV 240
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd14078  241 DPKKRITVKELLNHPWV 257
MELK_C cd12198
C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, ...
514-608 3.23e-49

C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, also called protein kinase 38 (PK38) or pEg3 kinase, is a cell cycle-regulated serine/threonine protein kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It is phosphorylated and maximally active during mitosis and is involved in regulating cell cycle progression, division, proliferation, tumor growth, and mRNA splicing. MELK shows a broad substrate specificity, including the zinc finger-like protein ZPR9, the transcription and splicing factor NIPP1, and the protein-tyrosine phosphatase Cdc25B, among others. MELK contains an N-terminal catalytic domain followed by a ubiquitin-associated (UBA) domain, a TP dipeptide-rich region, and a C-terminal KA1 domain. The KA1 domain of MELK, together with its TP dipeptide-rich region, functions as an autoinhibitory domain. The KA1 domain of the related microtubule affinity-regulating kinases (MARKs) has been shown to bind anionic phospholipids and may be involved in membrane localization.


:

Pssm-ID: 213383  Cd Length: 96  Bit Score: 165.87  E-value: 3.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 514 RRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKP-DVVGIRRQRLKG 592
Cdd:cd12198    1 RKVKALYNVSTTSSKDPEQVLNELKRVLAKKGIDCKQKGYTLRCKTKDDFGKVKLTFELEVCRLPGLdEVVGIRRKRLKG 80
                         90
                 ....*....|....*.
gi 375493532 593 DAWVYKRLVEDILSSC 608
Cdd:cd12198   81 DAWVYKKVCEDILRMA 96
UBA_MELK cd14341
UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, ...
281-332 2.81e-12

UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, also called protein kinase Eg3 (pEg3 kinase), protein kinase PK38 (PK38), or tyrosine-protein kinase MELK, is a cell cycle dependent protein kinase involved in diverse cell processes including stem cell renewal, cell cycle progression, cell proliferation, apoptosis and mRNA processing. It is expressed in normal tissues and especially in cancer cells. It is upregulated in cancer tissues and thus may act as potential anticancer target in diverse tumor entities. MELK comprises an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain, and a C-terminal autoinhibitory domain of 5'-AMP-activated protein kinase (AMPK).


:

Pssm-ID: 270526  Cd Length: 52  Bit Score: 61.45  E-value: 2.81e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 281 HLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRL 332
Cdd:cd14341    1 ELDEDCITELSVYYGKSREEMEQLIKEWKYDYLTATYLLLLDKKRRGKPVRL 52
 
Name Accession Description Interval E-value
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
7-263 0e+00

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: 575.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14078    1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd14078   81 EYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd14078  161 TCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQV 240
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd14078  241 DPKKRITVKELLNHPWV 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-263 1.70e-107

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 323.71  E-value: 1.70e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpKGNKDYHLQTCCG 170
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR--QLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF-DDDNVMALYKKIMRGKYDVPKW---LSPSSILLLQQMLQV 246
Cdd:smart00220 159 TPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVK 237
                          250
                   ....*....|....*..
gi 375493532   247 DPKKRISMKNLLNHPWI 263
Cdd:smart00220 238 DPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
11-263 3.06e-92

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 284.50  E-value: 3.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP-RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDkNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpKGNKDYHLQTCC 169
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAR--QLNSGSSLTTFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY---DVPKWLSPSSILLLQQMLQV 246
Cdd:pfam00069 159 GTPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKK 237
                         250
                  ....*....|....*..
gi 375493532  247 DPKKRISMKNLLNHPWI 263
Cdd:pfam00069 238 DPSKRLTATEALQHPWF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-355 7.79e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 191.11  E-value: 7.79e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHIltgEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQ-HICQLYHVLETANKIFMVLE 87
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLEskSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYI---ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY-HKLKLIDFGLCAKPKGNKD- 162
Cdd:COG0515   79 YVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKLLPDPGSt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 ----YHLQTCCGSLAYAAPELIQGKS--YLGSEADVWSMGILLYVLMCGFLPFDDDN----VMALYKKIMRGKY------ 226
Cdd:COG0515  159 ssipALPSTSVGTPGYMAPEVLLGLSlaYASSSSDIWSLGITLYELLTGLPPFEGEKnssaTSQTLKIILELPTpslasp 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 227 ---DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMED 303
Cdd:COG0515  239 lspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSL 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 304 LISLWQYDHLTATYLLLLAKKAR-GKPVRLRLSSFSCGQASATPFTDIKFTKY 355
Cdd:COG0515  319 AISGSDLKLDDSNFSKELAPNGVsSSPHNSSSLLLSTASSKRSSLPKISARSS 371
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
8-262 2.59e-50

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 176.93  E-value: 2.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYhl 165
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF-AKKVPDRTF-- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 qTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:PTZ00263 174 -TLCGTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQ 251
                        250       260
                 ....*....|....*....|..
gi 375493532 246 VDPKKRI-SMKN----LLNHPW 262
Cdd:PTZ00263 252 TDHTKRLgTLKGgvadVKNHPY 273
MELK_C cd12198
C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, ...
514-608 3.23e-49

C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, also called protein kinase 38 (PK38) or pEg3 kinase, is a cell cycle-regulated serine/threonine protein kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It is phosphorylated and maximally active during mitosis and is involved in regulating cell cycle progression, division, proliferation, tumor growth, and mRNA splicing. MELK shows a broad substrate specificity, including the zinc finger-like protein ZPR9, the transcription and splicing factor NIPP1, and the protein-tyrosine phosphatase Cdc25B, among others. MELK contains an N-terminal catalytic domain followed by a ubiquitin-associated (UBA) domain, a TP dipeptide-rich region, and a C-terminal KA1 domain. The KA1 domain of MELK, together with its TP dipeptide-rich region, functions as an autoinhibitory domain. The KA1 domain of the related microtubule affinity-regulating kinases (MARKs) has been shown to bind anionic phospholipids and may be involved in membrane localization.


Pssm-ID: 213383  Cd Length: 96  Bit Score: 165.87  E-value: 3.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 514 RRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKP-DVVGIRRQRLKG 592
Cdd:cd12198    1 RKVKALYNVSTTSSKDPEQVLNELKRVLAKKGIDCKQKGYTLRCKTKDDFGKVKLTFELEVCRLPGLdEVVGIRRKRLKG 80
                         90
                 ....*....|....*.
gi 375493532 593 DAWVYKRLVEDILSSC 608
Cdd:cd12198   81 DAWVYKKVCEDILRMA 96
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
11-219 1.27e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLA-CHILtGEMVAIKIMdKNTLGSD---LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAkDTRL-DRDVAVKVL-RPDLARDpefVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHlQ 166
Cdd:NF033483  87 EYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI-ARALSSTTMT-Q 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 167 T--CCGSLAYAAPELIQGkSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMA-LYK 219
Cdd:NF033483 165 TnsVLGTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVSvAYK 219
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-251 1.23e-18

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: 90.29  E-value: 1.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    33 TGEMVAIKIM--DKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA-NKIFMVLEYCPGGELFDYIISQDRLSEEET 109
Cdd:TIGR03903    2 TGHEVAIKLLrtDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   110 RVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKlKLIDFGLCAKPKGNKDYHLQTCC------GSLAYAAPEL 179
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtgVRPHA-KVLDFGIGTLLPGVRDADVATLTrttevlGTPTYCAPEQ 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493532   180 IQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDVPKWLSPSSI-LLLQQMLQVDPKKR 251
Cdd:TIGR03903  161 LRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGASVAeILYQQLSPVDVSLPPWIAGHPLgQVLRKALNKDPRQR 233
UBA_MELK cd14341
UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, ...
281-332 2.81e-12

UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, also called protein kinase Eg3 (pEg3 kinase), protein kinase PK38 (PK38), or tyrosine-protein kinase MELK, is a cell cycle dependent protein kinase involved in diverse cell processes including stem cell renewal, cell cycle progression, cell proliferation, apoptosis and mRNA processing. It is expressed in normal tissues and especially in cancer cells. It is upregulated in cancer tissues and thus may act as potential anticancer target in diverse tumor entities. MELK comprises an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain, and a C-terminal autoinhibitory domain of 5'-AMP-activated protein kinase (AMPK).


Pssm-ID: 270526  Cd Length: 52  Bit Score: 61.45  E-value: 2.81e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 281 HLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRL 332
Cdd:cd14341    1 ELDEDCITELSVYYGKSREEMEQLIKEWKYDYLTATYLLLLDKKRRGKPVRL 52
KA1 pfam02149
Kinase associated domain 1;
567-610 1.38e-11

Kinase associated domain 1;


Pssm-ID: 426623  Cd Length: 44  Bit Score: 59.41  E-value: 1.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 375493532  567 TMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV 610
Cdd:pfam02149   1 VVKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSELRL 44
 
Name Accession Description Interval E-value
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
7-263 0e+00

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: 575.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14078    1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd14078   81 EYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd14078  161 TCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQV 240
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd14078  241 DPKKRITVKELLNHPWV 257
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
11-262 1.76e-141

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: 410.76  E-value: 1.76e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLkEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyhLQTCC 169
Cdd:cd14003   82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSL--LKTFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPK 249
Cdd:cd14003  160 GTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPS 239
                        250
                 ....*....|...
gi 375493532 250 KRISMKNLLNHPW 262
Cdd:cd14003  240 KRITIEEILNHPW 252
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
11-262 8.05e-114

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: 340.01  E-value: 8.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLP-RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIkSLDMEeKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcakpkGN--KDYH-L 165
Cdd:cd14079   84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL-----SNimRDGEfL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd14079  159 KTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLV 238
                        250
                 ....*....|....*..
gi 375493532 246 VDPKKRISMKNLLNHPW 262
Cdd:cd14079  239 VDPLKRITIPEIRQHPW 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-262 3.36e-110

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: 330.98  E-value: 3.36e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSeDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKpKGNKDYHLQ 166
Cdd:cd05117   82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGL-AK-IFEEGEKLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK--W--LSPSSILLLQQ 242
Cdd:cd05117  160 TVCGTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSpeWknVSEEAKDLIKR 238
                        250       260
                 ....*....|....*....|
gi 375493532 243 MLQVDPKKRISMKNLLNHPW 262
Cdd:cd05117  239 LLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-263 1.70e-107

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 323.71  E-value: 1.70e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpKGNKDYHLQTCCG 170
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR--QLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF-DDDNVMALYKKIMRGKYDVPKW---LSPSSILLLQQMLQV 246
Cdd:smart00220 159 TPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVK 237
                          250
                   ....*....|....*..
gi 375493532   247 DPKKRISMKNLLNHPWI 263
Cdd:smart00220 238 DPEKRLTAEEALQHPFF 254
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
11-262 4.58e-99

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: 302.40  E-value: 4.58e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNK-DYHLQT 167
Cdd:cd14663   82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRqDGLLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVD 247
Cdd:cd14663  162 TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPN 241
                        250
                 ....*....|....*
gi 375493532 248 PKKRISMKNLLNHPW 262
Cdd:cd14663  242 PSTRITVEQIMASPW 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
11-263 2.63e-97

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: 297.63  E-value: 2.63e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKEsvLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA-KPKGNKdyhLQT 167
Cdd:cd14081   83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlQPEGSL---LET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVD 247
Cdd:cd14081  160 SCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVN 239
                        250
                 ....*....|....*.
gi 375493532 248 PKKRISMKNLLNHPWI 263
Cdd:cd14081  240 PEKRITIEEIKKHPWF 255
Pkinase pfam00069
Protein kinase domain;
11-263 3.06e-92

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 284.50  E-value: 3.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP-RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDkNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpKGNKDYHLQTCC 169
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAR--QLNSGSSLTTFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY---DVPKWLSPSSILLLQQMLQV 246
Cdd:pfam00069 159 GTPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKK 237
                         250
                  ....*....|....*..
gi 375493532  247 DPKKRISMKNLLNHPWI 263
Cdd:pfam00069 238 DPSKRLTATEALQHPWF 254
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
10-263 7.69e-92

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: 283.51  E-value: 7.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14071    1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLdEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcakpkGN---KDYHL 165
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF-----SNffkPGELL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd14071  156 KTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLV 235
                        250
                 ....*....|....*...
gi 375493532 246 VDPKKRISMKNLLNHPWI 263
Cdd:cd14071  236 LDPSKRLTIEQIKKHKWM 253
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
11-263 4.37e-89

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: 276.76  E-value: 4.37e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHI--LTGEMVAIKIMDKNTLGSD-----LPRiktEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKKKAPKDflekfLPR---ELEILRKLRHPNIIQVYSIFERGSKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDY 163
Cdd:cd14080   79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGF-ARLCPDDDG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HL--QTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP---KWLSPSSIL 238
Cdd:cd14080  158 DVlsKTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECKD 237
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14080  238 LIDQLLEPDPTKRATIEEILNHPWL 262
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
11-263 3.11e-87

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: 272.01  E-value: 3.11e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNT-----------LGSDLPR-IKTEIEALKN--LRHQHICQLYHVL 76
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkkerekrLEKEISRdIRTIREAALSslLNHPHICRLRDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  77 ETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcak 156
Cdd:cd14077   83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 pkGN---KDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLS 233
Cdd:cd14077  160 --SNlydPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLS 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14077  238 SECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
11-263 4.40e-86

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: 268.49  E-value: 4.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS--DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDeqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgnKDYHLQTC 168
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYS--KDKLLQTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSiLLLQQMLQVDP 248
Cdd:cd14073  161 CGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDAS-GLIRWMLTVNP 239
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14073  240 KRRATIEDIANHWWV 254
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
17-263 3.22e-85

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: 266.26  E-value: 3.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14007    8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLqKSGLEHqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyhLQTCCGSLAY 174
Cdd:cd14007   88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNR---RKTFCGTLDY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISM 254
Cdd:cd14007  165 LPPEMVEGKEY-DYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSL 243

                 ....*....
gi 375493532 255 KNLLNHPWI 263
Cdd:cd14007  244 EQVLNHPWI 252
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
11-263 3.71e-85

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: 266.31  E-value: 3.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNpSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-PKGNKdyhLQTC 168
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEfTPGNK---LDTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd14072  159 CGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNP 238
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14072  239 SKRGTLEQIMKDRWM 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
11-263 8.29e-83

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: 260.42  E-value: 8.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DDVSKahLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL-KLIDFGLCAKPKGNKdyHLQ 166
Cdd:cd14074   84 GDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQPGE--KLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd14074  162 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIR 241
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd14074  242 DPKKRASLEEIENHPWL 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
10-263 1.42e-82

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: 259.58  E-value: 1.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14075    3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRlLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgnKDYHLQTC 168
Cdd:cd14075   83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAK--RGETLNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd14075  161 CGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVP 240
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14075  241 SDRYSIDEIKNSEWL 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
17-263 1.02e-79

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: 252.47  E-value: 1.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL-------------GSDLPRIKTEIEALKNLRHQHICQLYHVLE--TANK 81
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLrkrregkndrgkiKNALDDVRREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGEL--FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKPKG 159
Cdd:cd14008   81 LYLVLEYCEGGPVmeLDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG-VSEMFE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCCGSLAYAAPELIQG--KSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK--YDVPKWLSPS 235
Cdd:cd14008  160 DGNDTLQKTAGTPAFLAPELCDGdsKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNdeFPIPPELSPE 239
                        250       260
                 ....*....|....*....|....*...
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14008  240 LKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
11-262 4.63e-77

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: 245.28  E-value: 4.63e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-----LPRiktEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDylqkfLPR---EIEVIKGLKHPNLICFYEAIETTSRVYII 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL---CAKPKGNKD 162
Cdd:cd14162   79 MELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFargVMKTKDGKP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQ 241
Cdd:cd14162  159 KLSETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRvVFPKNPTVSEECKDLIL 238
                        250       260
                 ....*....|....*....|.
gi 375493532 242 QMLqVDPKKRISMKNLLNHPW 262
Cdd:cd14162  239 RML-SPVKKRITIEEIKRDPW 258
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
17-262 7.67e-74

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: 236.64  E-value: 7.67e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIikRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSLAY 174
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA-KELSSDGDRTYTFCGTPEY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI-- 252
Cdd:cd05123  160 LAPEVLLGKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLgs 238
                        250
                 ....*....|.
gi 375493532 253 -SMKNLLNHPW 262
Cdd:cd05123  239 gGAEEIKAHPF 249
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-262 1.67e-72

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: 233.42  E-value: 1.67e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14083    3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKPKGNKDyhL 165
Cdd:cd14083   83 VTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGL-SKMEDSGV--M 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKW--LSPSSILLLQ 241
Cdd:cd14083  160 STACGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYefDSPYWddISDSAKDFIR 238
                        250       260
                 ....*....|....*....|.
gi 375493532 242 QMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14083  239 HLMEKDPNKRYTCEQALEHPW 259
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
6-263 3.60e-69

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: 225.35  E-value: 3.60e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   6 ELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-------GSDLPRIKTEIEALKNLRHQHICQLYHVLET 78
Cdd:cd14084    3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFtigsrreINKPRNIETEIEILKKLSHPCIIKIEDFFDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcA 155
Cdd:cd14084   83 EDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL-S 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNkDYHLQTCCGSLAYAAPELIQ--GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNV-MALYKKIMRGKYD-VPKW 231
Cdd:cd14084  162 KILGE-TSLMKTLCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTqMSLKEQILSGKYTfIPKA 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 232 ---LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14084  241 wknVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
11-263 4.22e-69

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: 224.45  E-value: 4.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHiLTGEMVAIKIMDKNTLG--SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRIKdeQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyHLQTC 168
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDK--FLQTY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSpSSILLLQQMLQVDP 248
Cdd:cd14161  162 CGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLMVNP 240
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14161  241 ERRATLEDVASHWWV 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
17-261 8.61e-69

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: 222.15  E-value: 8.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYA 175
Cdd:cd00180   81 LLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPYY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 176 APELIQGKSYLGSEADVWSMGILLYVLmcgflpfdddnvmalykkimrgkydvpkwlsPSSILLLQQMLQVDPKKRISMK 255
Cdd:cd00180  161 APPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRPSAK 209

                 ....*.
gi 375493532 256 NLLNHP 261
Cdd:cd00180  210 ELLEHL 215
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
17-262 2.57e-68

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: 222.10  E-value: 2.57e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQEnLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLL---FDEYHKLKLIDFGLcAKpkgnkdyHLQ------ 166
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLlstSGDDPVLKIADFGF-AR-------SLQpasmae 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG----KYDVPKWLSPSSILLLQQ 242
Cdd:cd14009  153 TLCGSPLYMAPEILQFQKY-DAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdaviPFPIAAQLSPDCKDLLRR 231
                        250       260
                 ....*....|....*....|
gi 375493532 243 MLQVDPKKRISMKNLLNHPW 262
Cdd:cd14009  232 LLRRDPAERISFEEFFAHPF 251
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
11-263 3.39e-68

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: 222.74  E-value: 3.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHI-----LTGEMVAIKIMDKNTLG--SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd14076    3 YILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRDTQQenCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd14076   83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKS-YLGSEADVWSMGILLYVLMCGFLPFDDD-------NVMALYKKIMRGKYDVPKWLSPS 235
Cdd:cd14076  163 LMSTSCGSPCYAAPELVVSDSmYAGRKADIWSCGVILYAMLAGYLPFDDDphnpngdNVPRLYRYICNTPLIFPEYVTPK 242
                        250       260
                 ....*....|....*....|....*...
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14076  243 ARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
9-263 5.46e-68

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: 221.66  E-value: 5.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPkqREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDYh 164
Cdd:cd14099   81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARleYDGERKK- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK--WLSPSSILLLQQ 242
Cdd:cd14099  160 --TLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPShlSISDEAKDLIRS 237
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14099  238 MLQPDPTKRPSLDEILSHPFF 258
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
11-262 8.18e-68

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: 222.45  E-value: 8.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlgsDLPR------IKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKA----KIIKlkqvehVLNEKRILSEVRHPFIVNLLGSFQDDRNLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYh 164
Cdd:cd05580   79 VMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGF-AKRVKDRTY- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd05580  157 --TLCGTPEYLAPEIILSKGH-GKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLL 233
                        250       260
                 ....*....|....*....|...
gi 375493532 245 QVDPKKRI-SMKN----LLNHPW 262
Cdd:cd05580  234 VVDLTKRLgNLKNgvedIKNHPW 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
11-262 9.60e-67

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: 218.35  E-value: 9.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH----KLKLIDFGLCAKPKGNkdyhLQ 166
Cdd:cd14095   82 GGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEP----LF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYDV--PKW--LSPSSILLL 240
Cdd:cd14095  158 TVCGTPTYVAPEILAETGY-GLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFEFlsPYWdnISDSAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14095  237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
11-262 2.81e-66

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: 217.34  E-value: 2.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKN-TLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRkVAGNDknLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLcAKPKGNkDYHL 165
Cdd:cd14098   82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGL-AKVIHT-GTFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSY-----LGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWL----SPSS 236
Cdd:cd14098  160 VTFCGTMAYLAPEILMSKEQnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfniSEEA 239
                        250       260
                 ....*....|....*....|....*.
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14098  240 IDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
11-262 5.73e-66

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: 216.43  E-value: 5.73e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPEnIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA--KPKGnKDYHLQT 167
Cdd:cd14069   83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATvfRYKG-KERLLNK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDD----DNVMALYKKIMRGKYDVPKWLSPSSILLLQQM 243
Cdd:cd14069  162 MCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQpsdsCQEYSDWKENKKTYLTPWKKIDTAALSLLRKI 241
                        250
                 ....*....|....*....
gi 375493532 244 LQVDPKKRISMKNLLNHPW 262
Cdd:cd14069  242 LTENPNKRITIEDIKKHPW 260
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
11-270 1.66e-65

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: 216.35  E-value: 1.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlGSDlPRikTEIEALknLR---HQHICQLYHVLETANKIFMVLE 87
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKS--KRD-PS--EEIEIL--LRygqHPNIITLRDVYDDGNSVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-DEYHK---LKLIDFGLcAKPKGNKDY 163
Cdd:cd14091   75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGF-AKQLRAENG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF---DDDNVMALYKKIMRGKYDV--PKW--LSPSS 236
Cdd:cd14091  154 LLMTPCYTANFVAPEVLKKQGYDAA-CDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARIGSGKIDLsgGNWdhVSDSA 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYP 270
Cdd:cd14091  233 KDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLP 266
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-251 3.57e-65

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: 214.37  E-value: 3.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP--RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFreRFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd14014   82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--------DVPKWLSPssilLL 240
Cdd:cd14014  162 LGTPAYMAPEQARGGP-VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsplnpDVPPALDA----II 236
                        250
                 ....*....|.
gi 375493532 241 QQMLQVDPKKR 251
Cdd:cd14014  237 LRALAKDPEER 247
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
11-263 6.54e-65

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: 213.53  E-value: 6.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD---LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL--CAKPKGNKDyHL 165
Cdd:cd14070   84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSD-PF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDD--NVMALYKKIMRGKYD-VPKWLSPSSILLLQQ 242
Cdd:cd14070  163 STQCGSPAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNpLPTDLSPGAISFLRS 241
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14070  242 LLEPDPLKRPNIKQALANRWL 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
11-262 1.01e-64

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: 213.37  E-value: 1.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-------IKTEIEALKNL-RHQHICQLYHVLETANKI 82
Cdd:cd14093    5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEaeelreaTRREIEILRQVsGHPNIIELHDVFESPTFI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL-CAKPKGNK 161
Cdd:cd14093   85 FLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFaTRLDEGEK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 dyhLQTCCGSLAYAAPELIQGKSYLGS-----EADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKW--L 232
Cdd:cd14093  165 ---LRELCGTPGYLAPEVLKCSMYDNApgygkEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYefGSPEWddI 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 233 SPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14093  242 SDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
15-263 2.62e-63

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: 209.30  E-value: 2.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKeVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKPKGNKDYH--LQTCCGS 171
Cdd:cd06606   86 LASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFG-CAKRLAEIATGegTKSLRGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRGKY--DVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd06606  165 PYWMAPEVIRGEGY-GRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEppPIPEHLSEEAKDFLRKCLQRDP 243
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd06606  244 KKRPTADELLQHPFL 258
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
17-262 1.21e-62

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: 207.84  E-value: 1.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDK-NTLGSDL-PRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKrDMIRKNQvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL--------------CAKPKGN 160
Cdd:cd05579   81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLskvglvrrqiklsiQKKSNGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK--WLSPSSIL 238
Cdd:cd05579  161 PEKEDRRIVGTPDYLAPEILLGQGH-GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKD 239
                        250       260
                 ....*....|....*....|....*..
gi 375493532 239 LLQQMLQVDPKKRI---SMKNLLNHPW 262
Cdd:cd05579  240 LISKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-263 3.11e-62

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: 207.67  E-value: 3.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHI-LTGEMVAIKIMDK------NTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKadlssdNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD------EYHKL----------- 146
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipSIVKLrkadddetkvd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 147 ----------------KLIDFGLCakpKGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD 210
Cdd:cd14096  163 egefipgvggggigivKLADFGLS---KQVWDSNTKTPCGTVGYTAPEVVKDERY-SKKVDMWALGCVLYTLLCGFPPFY 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 211 DDNVMALYKKIMRGKYDV--PKW--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14096  239 DESIETLTEKISRGDYTFlsPWWdeISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-266 3.42e-62

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: 207.05  E-value: 3.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD---EYHKLKLIDFGLcakPKGNKDYHLQT 167
Cdd:cd14169   85 GGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGL---SKIEAQGMLST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKW--LSPSSILLLQQM 243
Cdd:cd14169  162 ACGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYefDSPYWddISESAKDFIRHL 240
                        250       260
                 ....*....|....*....|...
gi 375493532 244 LQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd14169  241 LERDPEKRFTCEQALQHPWISGD 263
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
11-263 2.03e-61

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: 204.63  E-value: 2.03e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-----LPRiktEIEALKNLRHQHICQLYHVLETAN-KIFM 84
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfvekfLPR---ELEILARLNHKSIIKTYEIFETSDgKVYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL---CAKPKGNK 161
Cdd:cd14165   80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFskrCLRDENGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSIL--L 239
Cdd:cd14165  160 IVLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSECkdL 239
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14165  240 IYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
11-263 4.91e-61

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: 203.53  E-value: 4.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREV--CESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFdeYH-----KLKLIDFGLCAKPKGNKDYHL 165
Cdd:cd14087   81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLY--YHpgpdsKIMITDFGLASTRKKGPNCLM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY----DVPKWLSPSSILLLQ 241
Cdd:cd14087  159 KTTCGTPEYIAPEILLRKPYTQS-VDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYsysgEPWPSVSNLAKDFID 237
                        250       260
                 ....*....|....*....|..
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14087  238 RLLTVNPGERLSATQALKHPWI 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-263 1.10e-60

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: 202.57  E-value: 1.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKPKGNKDYhLQT 167
Cdd:cd14167   85 GGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYyslDEDSKIMISDFGL-SKIEGSGSV-MST 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKW--LSPSSILLLQQM 243
Cdd:cd14167  163 ACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYefDSPYWddISDSAKDFIQHL 241
                        250       260
                 ....*....|....*....|
gi 375493532 244 LQVDPKKRISMKNLLNHPWI 263
Cdd:cd14167  242 MEKDPEKRFTCEQALQHPWI 261
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
10-262 2.71e-60

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 201.33  E-value: 2.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14185    1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKLKLIDFGLC---AKPkgnkd 162
Cdd:cd14185   81 RGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAkyvTGP----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 yhLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYDV--PKW--LSPSS 236
Cdd:cd14185  156 --IFTVCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQLGHYEFlpPYWdnISEAA 232
                        250       260
                 ....*....|....*....|....*.
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14185  233 KDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-266 8.34e-60

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: 200.99  E-value: 8.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14166    3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRD-SSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcakPKGNKDYHL 165
Cdd:cd14166   82 VSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL---SKMEQNGIM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlgSEA-DVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV--PKW--LSPSSILLL 240
Cdd:cd14166  159 STACGTPGYVAPEVLAQKPY--SKAvDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFesPFWddISESAKDFI 236
                        250       260
                 ....*....|....*....|....*.
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd14166  237 RHLLEKNPSKRYTCEKALSHPWIIGN 262
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-263 1.43e-59

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: 199.23  E-value: 1.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSeKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSE--EETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHL 165
Cdd:cd08215   82 DGGDLAQKIKKQKKKGQpfPEEQILdwFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGI-SKVLESTTDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSSILLLQQML 244
Cdd:cd08215  161 KTVVGTPYYLSPELCENKPY-NYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSML 239
                        250
                 ....*....|....*....
gi 375493532 245 QVDPKKRISMKNLLNHPWI 263
Cdd:cd08215  240 QKDPEKRPSANEILSSPFI 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
17-262 8.92e-59

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: 197.45  E-value: 8.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIvQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKP--KGNKDYhlqTCCGSL 172
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFG-FAKKlgSGRKTW---TFCGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYDV--PKWLSPSSILLLQQMLQVDP 248
Cdd:cd05572  157 EYVAPEIILNKGY-DFSVDYWSLGILLYELLTGRPPFggDDEDPMKIYNIILKGIDKIefPKYIDKNAKNLIKQLLRRNP 235
                        250
                 ....*....|....*....
gi 375493532 249 KKRI-----SMKNLLNHPW 262
Cdd:cd05572  236 EERLgylkgGIRDIKKHKW 254
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
11-263 1.82e-58

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: 196.36  E-value: 1.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-----LPRiktEIEALKNLRHQHICQLYHVLETAN-KIFM 84
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEfiqrfLPR---ELQIVERLDHKNIIHVYEMLESADgKIYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYhKLKLIDFGLCAK-PKGNKDY 163
Cdd:cd14163   79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQlPKGGREL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HlQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGkYDVPKWLSPSSIL--LLQ 241
Cdd:cd14163  158 S-QTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHLGVSRTCqdLLK 235
                        250       260
                 ....*....|....*....|..
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14163  236 RLLEPDMVLRPSIEEVSWHPWL 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
17-262 2.95e-58

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: 195.56  E-value: 2.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNtlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKR--DKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDE--YHKLKLIDFGLcAKpKGNKDYHLQTCCGSLAY 174
Cdd:cd14006   79 RLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGL-AR-KLNPGEELKEIFGTPEF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGkSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV----PKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd14006  157 VAPEIVNG-EPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFseeyFSSVSQEAKDFIRKLLVKEPRK 235
                        250
                 ....*....|..
gi 375493532 251 RISMKNLLNHPW 262
Cdd:cd14006  236 RPTAQEALQHPW 247
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-264 1.70e-57

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: 195.60  E-value: 1.70e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YEL---HETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgsdlpRIKT--EIEALKNLR-HQHICQLYHVLETANKIFM 84
Cdd:cd14092    5 YELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSR--------RLDTsrEVQLLRLCQgHPNIVKLHEVFQDELHTYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGL-CAKPKGN 160
Cdd:cd14092   77 VMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFaRLKPENQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KdyhLQTCCGSLAYAAPELIQGKSYLG--SEA-DVWSMGILLYVLMCGFLPF----DDDNVMALYKKIMRGK--YDVPKW 231
Cdd:cd14092  157 P---LKTPCFTLPYAAPEVLKQALSTQgyDEScDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDfsFDGEEW 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 232 --LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIM 264
Cdd:cd14092  234 knVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-265 2.36e-57

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: 194.56  E-value: 2.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14086    3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSArDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKPKGNKDyHLQ 166
Cdd:cd14086   83 TGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADFGLAIEVQGDQQ-AWF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP--KW--LSPSSILLLQQ 242
Cdd:cd14086  162 GFAGTPGYLSPEVLRKDPY-GKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPspEWdtVTPEAKDLINQ 240
                        250       260
                 ....*....|....*....|...
gi 375493532 243 MLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd14086  241 MLTVNPAKRITAAEALKHPWICQ 263
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-266 5.51e-57

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: 194.11  E-value: 5.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   2 KDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANK 81
Cdd:cd14168    3 KQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKPK 158
Cdd:cd14168   83 LYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGL-SKME 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYhLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKW--LSP 234
Cdd:cd14168  162 GKGDV-MSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYefDSPYWddISD 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 235 SSILLLQQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd14168  240 SAKDFIRNLMEKDPNKRYTCEQALRHPWIAGD 271
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
17-263 2.05e-56

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: 191.37  E-value: 2.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHI--LTGEMVAIKIMDKNTLGSDLPRIKT----EIEALKNLRHQHICQLYHVLET-ANKIFMVLEYC 89
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRKDYVKrltsEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK---PKGNKDYHLQ 166
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVfgmPAEKESPMSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFD----DDNVMALYKKIMR---GKYDVPKWLSPS-SIL 238
Cdd:cd13994  161 GLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRsakkSDSAYKAYEKSGDftnGPYEPIENLLPSeCRR 240
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd13994  241 LIYRMLHPDPEKRITIDEALNDPWV 265
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
17-262 3.81e-56

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: 190.16  E-value: 3.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL-----GSDlpRIKTEIEALKNLRHQHICQLYHVL--ETANKIFMVLEYC 89
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLrripnGEA--NVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGG--ELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYHLQ 166
Cdd:cd14119   79 VGGlqEMLDSA-PDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAeALDLFAEDDTCT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQG-KSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd14119  158 TSQGSPAFQPPEIANGqDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLE 237
                        250
                 ....*....|....*..
gi 375493532 246 VDPKKRISMKNLLNHPW 262
Cdd:cd14119  238 KDPEKRFTIEQIRQHPW 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
10-263 4.22e-56

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: 190.11  E-value: 4.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESK-EKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpKGNKDYHLQTC 168
Cdd:cd05122   80 SGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSA--QLSDGKTRNTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd05122  158 VGTPYWMAPEVIQGKPY-GFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNgppGLRNPKKWSKEFKDFLKKCLQ 236
                        250
                 ....*....|....*...
gi 375493532 246 VDPKKRISMKNLLNHPWI 263
Cdd:cd05122  237 KDPEKRPTAEQLLKHPFI 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-355 7.79e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 191.11  E-value: 7.79e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHIltgEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQ-HICQLYHVLETANKIFMVLE 87
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLEskSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYI---ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY-HKLKLIDFGLCAKPKGNKD- 162
Cdd:COG0515   79 YVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKLLPDPGSt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 ----YHLQTCCGSLAYAAPELIQGKS--YLGSEADVWSMGILLYVLMCGFLPFDDDN----VMALYKKIMRGKY------ 226
Cdd:COG0515  159 ssipALPSTSVGTPGYMAPEVLLGLSlaYASSSSDIWSLGITLYELLTGLPPFEGEKnssaTSQTLKIILELPTpslasp 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 227 ---DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMED 303
Cdd:COG0515  239 lspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSL 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 304 LISLWQYDHLTATYLLLLAKKAR-GKPVRLRLSSFSCGQASATPFTDIKFTKY 355
Cdd:COG0515  319 AISGSDLKLDDSNFSKELAPNGVsSSPHNSSSLLLSTASSKRSSLPKISARSS 371
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
11-262 1.59e-54

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: 187.23  E-value: 1.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlgsdlpriktEIEALKNLRH----QHICQ----------LYHVL 76
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQ-----------KVVKLKQVEHtlneKRILQainfpflvklEYSFK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  77 ETANkIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd14209   72 DNSN-LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGnkdyHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSS 236
Cdd:cd14209  151 VKG----RTWTLCGTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDL 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 375493532 237 ILLLQQMLQVDPKKRI-SMKN----LLNHPW 262
Cdd:cd14209  226 KDLLRNLLQVDLTKRFgNLKNgvndIKNHKW 256
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
11-262 2.81e-54

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 185.88  E-value: 2.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPR------IKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDK----RHIIKekkvkyVTIEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKPKGNKDYH 164
Cdd:cd05581   79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFG-TAKVLGPDSSP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTC-----------------CGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD 227
Cdd:cd05581  158 ESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKP-AGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 375493532 228 VPKWLSPSSILLLQQMLQVDPKKRI------SMKNLLNHPW 262
Cdd:cd05581  237 FPENFPPDAKDLIQKLLVLDPSKRLgvnengGYDELKAHPF 277
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
11-262 1.11e-53

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: 183.69  E-value: 1.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY----HKLKLIDFGLCAKPKGNkdyhLQ 166
Cdd:cd14184   83 GGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYpdgtKSLKLGDFGLATVVEGP----LY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMA--LYKKIMRGKYDVPK--W--LSPSSILLL 240
Cdd:cd14184  159 TVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRSENNLQedLFDQILLGKLEFPSpyWdnITDSAKELI 237
                        250       260
                 ....*....|....*....|..
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14184  238 SHMLQVNVEARYTAEQILSHPW 259
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
9-263 1.57e-53

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: 183.52  E-value: 1.57e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14097    1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSsAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-----DEYHKL--KLIDFGLCAKPKGN 160
Cdd:cd14097   81 LCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiiDNNDKLniKVTDFGLSVQKYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG----KYDVPKWLSPSS 236
Cdd:cd14097  161 GEDMLQETCGTPIYMAPEVISAHGY-SQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGdltfTQSVWQSVSDAA 239
                        250       260
                 ....*....|....*....|....*..
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14097  240 KNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
10-263 3.01e-53

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: 182.59  E-value: 3.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-------LPRIKTEIEALKNLR---HQHICQLYHVLEta 79
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDtwvrdrkLGTVPLEIHILDTLNkrsHPNIVKLLDFFE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGE---LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd14004   79 DDEFYYLVMEKHGSgmdLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDYhlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDdnvmalYKKIMRGKYDVPKWLSPSS 236
Cdd:cd14004  159 IKSGPFD---TFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYN------IEEILEADLRIPYAVSEDL 229
                        250       260
                 ....*....|....*....|....*..
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14004  230 IDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-262 3.18e-53

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: 182.44  E-value: 3.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-----DLPRIKTEIEALK---NLRHQHICQLYHVLETANKI 82
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEwaminGPVPVPLEIALLLkasKPGVPGVIRLLDWYERPDGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEY-CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGlCAKP--- 157
Cdd:cd14005   82 LLIMERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG-CGALlkd 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKDYhlqtcCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDnvmalyKKIMRGKYDVPKWLSPSSI 237
Cdd:cd14005  161 SVYTDF-----DGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKECC 229
                        250       260
                 ....*....|....*....|....*
gi 375493532 238 LLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14005  230 DLISRCLQFDPSKRPSLEQILSHPW 254
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-263 5.60e-53

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: 183.10  E-value: 5.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14085    4 FFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV---DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLCAKPkgNKDYHLQ 166
Cdd:cd14085   81 TGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYatpAPDAPLKIADFGLSKIV--DQQVTMK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF-DDDNVMALYKKIMRGKYDV--PKW--LSPSSILLLQ 241
Cdd:cd14085  159 TVCGTPGYCAPEILRGCAY-GPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDFvsPWWddVSLNAKDLVK 237
                        250       260
                 ....*....|....*....|..
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14085  238 KLIVLDPKKRLTTQQALQHPWV 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
11-263 1.23e-52

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: 180.91  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14002    3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGgELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCC 169
Cdd:cd14002   83 QG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGF-ARAMSCNTLVLTSIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPK 249
Cdd:cd14002  161 GTPLYMAPELVQEQPY-DHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDPS 239
                        250
                 ....*....|....
gi 375493532 250 KRISMKNLLNHPWI 263
Cdd:cd14002  240 KRLSWPDLLEHPFV 253
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
17-259 2.07e-52

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: 180.04  E-value: 2.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd13999    1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEDDNDELLKeFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCCGSLAY 174
Cdd:cd13999   79 DLLHKKKIPLSWSLRLKIaLDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGL-SRIKNSTTEKMTGVVGTPRW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlgSE-ADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRGKY-DVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd13999  158 MAPEVLRGEPY--TEkADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKGLRpPIPPDCPPELSKLIKRCWNEDPEKR 235

                 ....*...
gi 375493532 252 ISMKNLLN 259
Cdd:cd13999  236 PSFSEIVK 243
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
10-263 3.15e-52

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: 180.38  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDK-----NTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd14105    6 FYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKrrskaSRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDE----YHKLKLIDFGLCAKPKGN 160
Cdd:cd14105   86 ILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKIEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYhlQTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV-PKWLSPSSIL- 238
Cdd:cd14105  166 NEF--KNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFdDEYFSNTSELa 242
                        250       260
                 ....*....|....*....|....*..
gi 375493532 239 --LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14105  243 kdFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
11-262 1.28e-51

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: 181.33  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPR------IKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRK----SDMLKreqiahVRAERDILADADSPWIVRLHYAFQDEDHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD-- 162
Cdd:cd05573   79 VMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDre 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 --------------------------YHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMA 216
Cdd:cd05573  159 sylndsvntlfqdnvlarrrphkqrrVRAYSAVGTPDYIAPEVLRGTGY-GPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 217 LYKKIMRGKY-----DVPKWlSPSSILLLQQMLqVDPKKRI-SMKNLLNHPW 262
Cdd:cd05573  238 TYSKIMNWKEslvfpDDPDV-SPEAIDLIRRLL-CDPEDRLgSAEEIKAHPF 287
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-262 5.31e-51

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: 177.63  E-value: 5.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPRIK------TEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAI----PEVIRLKqeqhvhNEKRVLKEVSHPFIIRLFWTEHDQRFLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYh 164
Cdd:cd05612   79 LMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF-AKKLRDRTW- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd05612  157 --TLCGTPEYLAPEVIQSKGH-NKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLL 233
                        250       260
                 ....*....|....*....|...
gi 375493532 245 QVDPKKRI-SMKN----LLNHPW 262
Cdd:cd05612  234 VVDRTRRLgNMKNgaddVKNHRW 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-263 6.66e-51

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: 176.77  E-value: 6.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYEL-HETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-LPRIKTEIEALK-NLRHQHICQLYHVLETANK 81
Cdd:cd14106    3 ENINEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDcRNEILHEIAVLElCKDCPRVVNLHEVYETRSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGL-CAKP 157
Cdd:cd14106   83 LILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGIsRVIG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNkdyHLQTCCGSLAYAAPELIqgkSY--LGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP----KW 231
Cdd:cd14106  163 EGE---EIREILGTPDYVAPEIL---SYepISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPeelfKD 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 232 LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14106  237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
11-262 2.01e-50

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: 175.17  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlGSDL-PRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIER---GEKIdENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD--EYHKLKLIDFG------LCAKPKgnk 161
Cdd:cd14665   79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGyskssvLHSQPK--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 dyhlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKK----IMRGKYDVPKW--LSPS 235
Cdd:cd14665  156 -----STVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKtiqrILSVQYSIPDYvhISPE 230
                        250       260
                 ....*....|....*....|....*..
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14665  231 CRHLISRIFVADPATRITIPEIRNHEW 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
8-262 2.59e-50

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 176.93  E-value: 2.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYhl 165
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF-AKKVPDRTF-- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 qTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:PTZ00263 174 -TLCGTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQ 251
                        250       260
                 ....*....|....*....|..
gi 375493532 246 VDPKKRI-SMKN----LLNHPW 262
Cdd:PTZ00263 252 TDHTKRLgTLKGgvadVKNHPY 273
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
11-262 3.39e-50

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: 174.57  E-value: 3.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlGSDL-PRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIER---GLKIdENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD--EYHKLKLIDFG------LCAKPKgnk 161
Cdd:cd14662   79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGyskssvLHSQPK--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 dyhlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDD----DNVMALYKKIMRGKYDVPKW--LSPS 235
Cdd:cd14662  156 -----STVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQYKIPDYvrVSQD 230
                        250       260
                 ....*....|....*....|....*..
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14662  231 CRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
10-259 1.04e-49

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: 173.31  E-value: 1.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNL-------RHQHICQLYHVLETANKI 82
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQLREIdlhrrvsRHPNIITLHDVFETEVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKG 159
Cdd:cd13993   81 YIVLEYCPNGDLFEAITENRIyvGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLATTEKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYhlqtCCGSLAYAAPELI-----QGKSYLGSEADVWSMGILLYVLMCGFLPF-----DDDNVMALYKKIMrGKYDVP 229
Cdd:cd13993  161 SMDF----GVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWkiaseSDPIFYDYYLNSP-NLFDVI 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 230 KWLSPSSILLLQQMLQVDPKKRISMKNLLN 259
Cdd:cd13993  236 LPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
MELK_C cd12198
C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, ...
514-608 3.23e-49

C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, also called protein kinase 38 (PK38) or pEg3 kinase, is a cell cycle-regulated serine/threonine protein kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It is phosphorylated and maximally active during mitosis and is involved in regulating cell cycle progression, division, proliferation, tumor growth, and mRNA splicing. MELK shows a broad substrate specificity, including the zinc finger-like protein ZPR9, the transcription and splicing factor NIPP1, and the protein-tyrosine phosphatase Cdc25B, among others. MELK contains an N-terminal catalytic domain followed by a ubiquitin-associated (UBA) domain, a TP dipeptide-rich region, and a C-terminal KA1 domain. The KA1 domain of MELK, together with its TP dipeptide-rich region, functions as an autoinhibitory domain. The KA1 domain of the related microtubule affinity-regulating kinases (MARKs) has been shown to bind anionic phospholipids and may be involved in membrane localization.


Pssm-ID: 213383  Cd Length: 96  Bit Score: 165.87  E-value: 3.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 514 RRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKP-DVVGIRRQRLKG 592
Cdd:cd12198    1 RKVKALYNVSTTSSKDPEQVLNELKRVLAKKGIDCKQKGYTLRCKTKDDFGKVKLTFELEVCRLPGLdEVVGIRRKRLKG 80
                         90
                 ....*....|....*.
gi 375493532 593 DAWVYKRLVEDILSSC 608
Cdd:cd12198   81 DAWVYKKVCEDILRMA 96
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
11-263 7.29e-49

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: 170.81  E-value: 7.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLqT 167
Cdd:cd14186   83 CHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF-T 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPElIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVD 247
Cdd:cd14186  162 MCGTPNYISPE-IATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                        250
                 ....*....|....*.
gi 375493532 248 PKKRISMKNLLNHPWI 263
Cdd:cd14186  241 PADRLSLSSVLDHPFM 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
15-262 7.73e-49

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: 170.55  E-value: 7.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHI-LTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd14121    1 EKLGSGTYATVYKAYRKsGAREVVAVKCVSKSSLNkASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK--LKLIDFGLcAKPKGNKDyHLQTCCG 170
Cdd:cd14121   81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGF-AQHLKPND-EAHSLRG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK-YDVPKW--LSPSSILLLQQMLQVD 247
Cdd:cd14121  159 SPLYMAPEMILKKKY-DARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQRD 237
                        250
                 ....*....|....*
gi 375493532 248 PKKRISMKNLLNHPW 262
Cdd:cd14121  238 PDRRISFEEFFAHPF 252
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
10-263 9.38e-49

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: 171.44  E-value: 9.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLpRIKTEIEALKNLR-HQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14090    3 YKLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRS-RVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKPKGNKDY-- 163
Cdd:cd14090   82 MRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSSTSmt 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 -----HLQTCCGSLAYAAPELI-----QGKSYlGSEADVWSMGILLYVLMCGFLPF-----------------DDDNVma 216
Cdd:cd14090  162 pvttpELLTPVGSAEYMAPEVVdafvgEALSY-DKRCDLWSLGVILYIMLCGYPPFygrcgedcgwdrgeacqDCQEL-- 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 217 LYKKIMRGKYDVP--KW--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14090  239 LFHSIQEGEYEFPekEWshISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
11-263 1.35e-48

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: 170.10  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd06627    2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIpKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyHLQTCC 169
Cdd:cd06627   82 ENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEK-DENSVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd06627  161 GTPYWMAPEVIEMSGV-TTASDIWSVGCTVIELLTGNPPYYDLQPMaALFRIVQDDHPPLPENISPELRDFLLQCFQKDP 239
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd06627  240 TLRPSAKELLKHPWL 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-263 2.25e-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: 169.64  E-value: 2.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYH--VLETANKIFMVLE 87
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEkEKQQLVSEVNILRELKHPNIVRYYDriVDRANTTLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYI--ISQDRLSEEETRV--VFRQIVSAVAYVHSQGYA-----HRDLKPENLLFDEYHKLKLIDFGLcAKPK 158
Cdd:cd08217   82 YCEGGDLAQLIkkCKKENQYIPEEFIwkIFTQLLLALYECHNRSVGggkilHRDLKPANIFLDSDNNVKLGDFGL-ARVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTCCGSLAYAAPELIQGKSYlgSE-ADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSS 236
Cdd:cd08217  161 SHDSSFAKTYVGTPYYMSPELLNEQSY--DEkSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRYSSEL 238
                        250       260
                 ....*....|....*....|....*..
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd08217  239 NEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
5-263 2.36e-48

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: 169.81  E-value: 2.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDK-----NTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA 79
Cdd:cd14194    1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrtksSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH----KLKLIDFGLCA 155
Cdd:cd14194   81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNKDYhlQTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK-WLSP 234
Cdd:cd14194  161 KIDFGNEF--KNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeYFSN 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 235 SSIL---LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14194  238 TSALakdFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
11-266 2.92e-48

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: 169.79  E-value: 2.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14183    8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH----KLKLIDFGLCAKPKGNkdyhLQ 166
Cdd:cd14183   88 GGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGLATVVDGP----LY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYDVPK--W--LSPSSILLL 240
Cdd:cd14183  164 TVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDFPSpyWdnVSDSAKELI 242
                        250       260
                 ....*....|....*....|....*.
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd14183  243 TMMLQVDVDQRYSALQVLEHPWVNDD 268
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
17-263 8.10e-48

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: 167.79  E-value: 8.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAK-DREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDyhLQTCCGSLA 173
Cdd:cd14103   80 RVVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCvsRTGNQIKIIDFGLARKYDPDKK--LKVLFGTPE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 174 YAAPELIqgkSY--LGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV--PKW--LSPSSILLLQQMLQVD 247
Cdd:cd14103  158 FVAPEVV---NYepISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFddEAFddISDEAKDFISKLLVKD 234
                        250
                 ....*....|....*.
gi 375493532 248 PKKRISMKNLLNHPWI 263
Cdd:cd14103  235 PRKRMSAAQCLQHPWL 250
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
17-261 1.41e-47

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: 167.16  E-value: 1.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHI-LTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd14120    1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHK-------LKLIDFGLcAKpkgnkdyHLQ 166
Cdd:cd14120   81 DYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshNSGRKpspndirLKIADFGF-AR-------FLQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 ------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMAL---YKKIMRGKYDVPKWLSPSSI 237
Cdd:cd14120  153 dgmmaaTLCGSPMYMAPEVIMSLQY-DAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALK 231
                        250       260
                 ....*....|....*....|....
gi 375493532 238 LLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14120  232 DLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
17-263 4.47e-47

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: 166.38  E-value: 4.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL----------------------GSDLPRIKTEIEALKNLRHQHICQLYH 74
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgalgkpLDPLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  75 VLETANK--IFMVLEYCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG 152
Cdd:cd14118   82 VLDDPNEdnLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 153 LCAKPKGNkDYHLQTCCGSLAYAAPELIQG--KSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK 230
Cdd:cd14118  161 VSNEFEGD-DALLSSTAGTPAFMAPEALSEsrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPD 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 231 WLSPSSIL--LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14118  240 DPVVSEQLkdLILRMLDKNPSERITLPEIKEHPWV 274
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
15-262 8.54e-47

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: 165.54  E-value: 8.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVkLAC-HILTGEMVAIKIMDKNtlgsdlPRIKTEIEA-LKNLRHQHICQLYHVLETANK----IFMVLEY 88
Cdd:cd14089    7 QVLGLGINGKV-LECfHKKTGEKFALKVLRDN------PKARREVELhWRASGCPHIVRIIDVYENTYQgrkcLLVVMEC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIisQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKPKGNK 161
Cdd:cd14089   80 MEGGELFSRI--QERadsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTTKK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMAL----YKKIMRGKYDVP--KW--LS 233
Cdd:cd14089  158 S--LQTPCYTPYYVAPEVLGPEKYDKS-CDMWSLGVIMYILLCGYPPFYSNHGLAIspgmKKRIRNGQYEFPnpEWsnVS 234
                        250       260
                 ....*....|....*....|....*....
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14089  235 EEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
8-263 2.32e-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: 163.97  E-value: 2.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL---GSDlPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLekaGVE-HQLRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyh 164
Cdd:cd14116   83 ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRR-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd14116  161 -TTLCGTLDYLPPEMIEGRMH-DEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLL 238
                        250
                 ....*....|....*....
gi 375493532 245 QVDPKKRISMKNLLNHPWI 263
Cdd:cd14116  239 KHNPSQRPMLREVLEHPWI 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
11-270 3.46e-46

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: 164.81  E-value: 3.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSdlpriKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDP-----SEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-DEY---HKLKLIDFGLCAKPKGNKDYhL 165
Cdd:cd14175   78 RGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvDESgnpESLRICDFGFAKQLRAENGL-L 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDD---DNVMALYKKIMRGKYDVP--KW--LSPSSIL 238
Cdd:cd14175  157 MTPCYTANFVAPEVLKRQGY-DEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKFTLSggNWntVSDAAKD 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWIMQDYNYP 270
Cdd:cd14175  236 LVSKMLHVDPHQRLTAKQVLQHPWITQKDKLP 267
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
6-262 1.01e-45

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: 163.22  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   6 ELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMD---KNTLGSDLPRIKT----EIEALKNLR-HQHICQLYHVLE 77
Cdd:cd14181    7 EFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaERLSPEQLEEVRSstlkEIHILRQVSgHPSIITLIDSYE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  78 TANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL-CAK 156
Cdd:cd14181   87 SSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCHL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKdyhLQTCCGSLAYAAPELI-----QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV--P 229
Cdd:cd14181  167 EPGEK---LRELCGTPGYLAPEILkcsmdETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssP 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 230 KWLSPSSIL--LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14181  244 EWDDRSSTVkdLISRLLVVDPEIRLTAEQALQHPF 278
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
17-274 1.25e-45

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: 164.02  E-value: 1.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIiaKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSLAY 174
Cdd:cd05595   83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC-KEGITDGATMKTFCGTPEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI-- 252
Cdd:cd05595  162 LAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLgg 240
                        250       260
                 ....*....|....*....|....*
gi 375493532 253 ---SMKNLLNHPWIMQdynypVEWQ 274
Cdd:cd05595  241 gpsDAKEVMEHRFFLS-----INWQ 260
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
11-265 3.15e-45

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: 161.62  E-value: 3.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRiktEIEALKN--------LR----HQHICQLYHVLET 78
Cdd:cd14182    5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPE---EVQELREatlkeidiLRkvsgHPNIIQLKDTYET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL-CAKP 157
Cdd:cd14182   82 NTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFsCQLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKdyhLQTCCGSLAYAAPELIQ-----GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV--PK 230
Cdd:cd14182  162 PGEK---LREVCGTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPE 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 375493532 231 WLSPSSIL--LLQQMLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd14182  239 WDDRSDTVkdLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
17-260 3.54e-45

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: 160.86  E-value: 3.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQRekIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgNKDYHLQTCCGSLAY 174
Cdd:cd14189   89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLE-PPEQRKKTICGTPNY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISM 254
Cdd:cd14189  168 LAPEVLLRQGH-GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTL 246

                 ....*.
gi 375493532 255 KNLLNH 260
Cdd:cd14189  247 DQILEH 252
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
8-263 7.72e-45

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: 160.06  E-value: 7.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKfIMTPHESDKET--VRKEIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD--EYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd14114   79 EFLSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKESV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTccGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP----KWLSPSSILL 239
Cdd:cd14114  159 KVTT--GTAEFAAPEIVEREP-VGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDF 235
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14114  236 IRKLLLADPNKRMTIHQALEHPWL 259
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
11-283 8.81e-45

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: 160.95  E-value: 8.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGsdlPRIKTEIeALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRD---PSEEIEI-LLRYGQHPNIITLKDVYDDGKFVYLVMELMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-DEY---HKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:cd14178   81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmDESgnpESIRICDFGF-AKQLRAENGLLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF---DDDNVMALYKKIMRGKYDVP--KW--LSPSSILL 239
Cdd:cd14178  160 TPCYTANFVAPEVLKRQGY-DAACDIWSLGILLYTMLAGFTPFangPDDTPEEILARIGSGKYALSggNWdsISDAAKDI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWIMQDynypvEWQSKNPFIHLD 283
Cdd:cd14178  239 VSKMLHVDPHQRLTAPQVLRHPWIVNR-----EYLSQNQLSRQD 277
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
17-274 9.89e-45

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: 161.75  E-value: 9.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEVIiaKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FdYIISQDRL-SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpKGNKDY--HLQTCCGS 171
Cdd:cd05571   83 F-FHLSRERVfSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC---KEEISYgaTTKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd05571  159 PEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
                        250       260
                 ....*....|....*....|....*...
gi 375493532 252 I-----SMKNLLNHPWIMqdynyPVEWQ 274
Cdd:cd05571  238 LgggprDAKEIMEHPFFA-----SINWD 260
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
10-263 1.24e-44

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: 159.74  E-value: 1.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDK-----NTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd14196    6 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsraSRRGVSREEIEREVSILRQVLHPNIITLHDVYENRTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPEN-LLFDE---YHKLKLIDFGLCAKPKGN 160
Cdd:cd14196   86 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKnipIPHIKLIDFGLAHEIEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYhlQTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV-PKWLSPSSIL- 238
Cdd:cd14196  166 VEF--KNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSHTSELa 242
                        250       260
                 ....*....|....*....|....*..
gi 375493532 239 --LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14196  243 kdFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
10-263 1.27e-44

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: 159.78  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-----GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd14195    6 HYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH----KLKLIDFGLCAKPKGN 160
Cdd:cd14195   86 ILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKIEAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYhlQTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV-PKWLSPSSIL- 238
Cdd:cd14195  166 NEF--KNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFdEEYFSNTSELa 242
                        250       260
                 ....*....|....*....|....*..
gi 375493532 239 --LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14195  243 kdFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-293 1.58e-44

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: 160.98  E-value: 1.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYEL---HETIGTGGFAKVKLACHILTGEMVAIKI----MDKNTlgsdlpriKTEIEALKNLR-HQHICQLYHVLETAN 80
Cdd:cd14179    4 QHYELdlkDKPLGEGSFSICRKCLHKKTNQEYAVKIvskrMEANT--------QREIAALKLCEgHPNIVKLHEVYHDQL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLCA-K 156
Cdd:cd14179   76 HTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARlK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFD--DDNVMA-----LYKKIMRGKYDV- 228
Cdd:cd14179  156 PPDNQP--LKTPCFTLHYAAPELLNYNGYDES-CDLWSLGVILYTMLSGQVPFQchDKSLTCtsaeeIMKKIKQGDFSFe 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 229 -PKW--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYpvewqSKNPFIHLDDDCVTELSVH 293
Cdd:cd14179  233 gEAWknVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQL-----SSNPLMTPDILGSSGASVH 295
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
17-263 4.46e-44

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: 158.14  E-value: 4.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMdkNTLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTGKIYALKKI--HVDGDEEFRkqLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGY-AHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCCGSLA 173
Cdd:cd06623   87 ADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHiIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQC-NTFVGTVT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 174 YAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNV---MALYKKIMRGkyDVPKW----LSPSSILLLQQMLQV 246
Cdd:cd06623  166 YMSPERIQGESY-SYAADIWSLGLTLLECALGKFPFLPPGQpsfFELMQAICDG--PPPSLpaeeFSPEFRDFISACLQK 242
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd06623  243 DPKKRPSAAELLQHPFI 259
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
11-263 6.13e-44

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: 158.65  E-value: 6.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELH-ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLR-HQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14173    3 YQLQeEVLGEGAYARVQTCINLITNKEYAVKIIEKRP-GHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL---KLIDFGLCAKPKGNKDY-- 163
Cdd:cd14173   82 MRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKLNSDCsp 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 ----HLQTCCGSLAYAAPELIQG----KSYLGSEADVWSMGILLYVLMCGFLPF----------DDDNVMA-----LYKK 220
Cdd:cd14173  162 istpELLTPCGSAEYMAPEVVEAfneeASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgwDRGEACPacqnmLFES 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 221 IMRGKYDVPK--W--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14173  242 IQEGKYEFPEkdWahISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
17-251 9.07e-44

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: 158.92  E-value: 9.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTE--IEALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIieDDDVECTMTEkrVLALAN-RHPFLTGLHACFQTEDRLYFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKP-KGNKDYHlqTCCGS 171
Cdd:cd05570   82 DLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGiWGGNTTS--TFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd05570  160 PDYIAPEILREQDY-GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARR 238
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-263 1.14e-43

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: 156.63  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLR----HQHICQLYHVLET--ANKIFM 84
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPK--AALREIKLLKHLNdvegHPNIVKLLDVFEHrgGNHLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCpGGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH-KLKLIDFGLC--AKPKGN 160
Cdd:cd05118   79 VFELM-GMNLYELIkDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLArsFTSPPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYhLQTccgsLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRgkydvpkWLSPSSIL-L 239
Cdd:cd05118  158 TPY-VAT----RWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-------LLGTPEALdL 225
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd05118  226 LSKMLKYDPAKRITASQALAHPYF 249
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
11-262 1.93e-43

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: 158.16  E-value: 1.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPR------IKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRK----SEMLEkeqvahVRAERDILAEADNPWVVKLYYSFQDEENLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpKGNKDYH 164
Cdd:cd05599   79 IMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLC---TGLKKSH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQ-TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY------DVPkwLSPSSI 237
Cdd:cd05599  156 LAySTVGTPDYIAPEVFLQKGY-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWREtlvfppEVP--ISPEAK 232
                        250       260
                 ....*....|....*....|....*...
gi 375493532 238 LLLQQMLqVDPKKRI---SMKNLLNHPW 262
Cdd:cd05599  233 DLIERLL-CDAEHRLganGVEEIKSHPF 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
11-263 3.46e-43

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: 155.49  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNT-LGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKcIEKDSVRnVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyHLQTC 168
Cdd:cd05578   82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGT--LATST 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD------DDNVMALYKKIMRgkyDVPKWLSPSSILLLQQ 242
Cdd:cd05578  160 SGTKPYMAPEVFMRAGY-SFAVDWWSLGVTAYEMLRGKRPYEihsrtsIEEIRAKFETASV---LYPAGWSEEAIDLINK 235
                        250       260
                 ....*....|....*....|..
gi 375493532 243 MLQVDPKKRIS-MKNLLNHPWI 263
Cdd:cd05578  236 LLERDPQKRLGdLSDLKNHPYF 257
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
17-252 5.84e-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: 156.80  E-value: 5.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLA---CHILTGEMVAIKIMDKNTLGS---DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05584    4 LGKGGYGKVFQVrktTGSDKGKIFAMKVLKKASIVRnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYLS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCG 170
Cdd:cd05584   84 GGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC-KESIHDGTVTHTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd05584  163 TIEYMAPEILT-RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSS 241

                 ..
gi 375493532 251 RI 252
Cdd:cd05584  242 RL 243
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
11-263 9.63e-43

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: 154.41  E-value: 9.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14088    3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFdeYHKLK-----LIDFGLCAKPKGnkdyHL 165
Cdd:cd14088   83 GREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVY--YNRLKnskivISDFHLAKLENG----LI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIqGKSYLGSEADVWSMGILLYVLMCGFLPF----DDDNVMA----LYKKIMRGKY--DVPKW--LS 233
Cdd:cd14088  157 KEPCGTPEYLAPEVV-GRQRYGRPVDCWAIGVIMYILLSGNPPFydeaEEDDYENhdknLFRKILAGDYefDSPYWddIS 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14088  236 QAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
17-259 1.32e-42

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: 154.41  E-value: 1.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLgSDLPRIKTEIEALKNL-RHQHICQLYH--VLETANK--IFMVLEYCPG 91
Cdd:cd13985    8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDE-EQLRVAIKEIEIMKRLcGHPNIVQYYDsaILSSEGRkeVLLLMEYCPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 gELFDYIIS--QDRLSEEETRVVFRQIVSAVAYVHSQG--YAHRDLKPENLLFDEYHKLKLIDFGLCAkpkgNKDYHLQT 167
Cdd:cd13985   87 -SLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAT----TEHYPLER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCG------------SLAYAAPELIQGKSYL--GSEADVWSMGILLYVLMCGFLPFDDDNVMalykKIMRGKYDVPKW-- 231
Cdd:cd13985  162 AEEvniieeeiqkntTPMYRAPEMIDLYSKKpiGEKADIWALGCLLYKLCFFKLPFDESSKL----AIVAGKYSIPEQpr 237
                        250       260
                 ....*....|....*....|....*...
gi 375493532 232 LSPSSILLLQQMLQVDPKKRISMKNLLN 259
Cdd:cd13985  238 YSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
11-270 2.10e-42

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: 155.95  E-value: 2.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGsdlPRIKTEIeALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-DEY---HKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:cd14176   97 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESgnpESIRICDFGF-AKQLRAENGLLM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF---DDDNVMALYKKIMRGKYDVPK--WLSPSSIL--L 239
Cdd:cd14176  176 TPCYTANFVAPEVLERQGY-DAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGgyWNSVSDTAkdL 254
                        250       260       270
                 ....*....|....*....|....*....|.
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWIMQDYNYP 270
Cdd:cd14176  255 VSKMLHVDPHQRLTAALVLRHPWIVHWDQLP 285
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
9-260 2.77e-42

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: 152.86  E-value: 2.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14188    1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQRekIDKEIELHRILHHKHVVQFYHYFEDKENIYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDyh 164
Cdd:cd14188   81 EYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARlePLEHRR-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd14188  159 -RTICGTPNYLSPEVLNKQGH-GCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASML 236
                        250
                 ....*....|....*.
gi 375493532 245 QVDPKKRISMKNLLNH 260
Cdd:cd14188  237 SKNPEDRPSLDEIIRH 252
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
11-263 3.25e-42

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: 153.24  E-value: 3.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACH-ILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH---------KLKLIDFGLCAKPKGN 160
Cdd:cd14201   88 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYLQSN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 kdYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMAL---YKKIMRGKYDVPKWLSPSSI 237
Cdd:cd14201  168 --MMAATLCGSPMYMAPEVIMSQHY-DAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRETSPYLA 244
                        250       260
                 ....*....|....*....|....*.
gi 375493532 238 LLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14201  245 DLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
17-263 4.19e-42

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: 152.86  E-value: 4.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEM-VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD---------EYHKLKLIDFGLCAKPKGNKdyHLQ 166
Cdd:cd14202   90 DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQNNM--MAA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGsEADVWSMGILLYVLMCGFLPFDDDNVMAL---YKKIMRGKYDVPKWLSPSSILLLQQM 243
Cdd:cd14202  168 TLCGSPMYMAPEVIMSQHYDA-KADLWSIGTIIYQCLTGKAPFQASSPQDLrlfYEKNKSLSPNIPRETSSHLRQLLLGL 246
                        250       260
                 ....*....|....*....|
gi 375493532 244 LQVDPKKRISMKNLLNHPWI 263
Cdd:cd14202  247 LQRNQKDRMDFDEFFHHPFL 266
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
16-274 4.25e-42

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: 154.40  E-value: 4.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  16 TIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgsdlpRIKTE---IEA-----LKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAI-----LKRNEvkhIMAernvlLKNVKHPFLVGLHYSFQTKDKLYFVLD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKDyh 164
Cdd:cd05575   77 YVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKegiEPSDTTS-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd05575  155 --TFCGTPEYLAPEVLRKQPY-DRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLL 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 245 QVDPKKRISMKN----LLNHPWIMqdynyPVEWQ 274
Cdd:cd05575  232 QKDRTKRLGSGNdfleIKNHSFFR-----PINWD 260
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
15-263 8.41e-42

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: 152.88  E-value: 8.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLR-HQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNA-GHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKPKGNKDY------H 164
Cdd:cd14174   87 ILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFDLGSGVKLNSACtpittpE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQ----GKSYLGSEADVWSMGILLYVLMCGFLPF----------DDDNVM-----ALYKKIMRGK 225
Cdd:cd14174  167 LTTPCGSAEYMAPEVVEvftdEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgwDRGEVCrvcqnKLFESIQEGK 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 375493532 226 YDVPK--W--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14174  247 YEFPDkdWshISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
17-263 2.05e-41

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: 150.92  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM-----DKNTLgsdlPRIKTEIEALKNLRHQHICQLYHVLETANK--IFMvlEYC 89
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIrfqdnDPKTI----KEIADEMKVLEGLDHPNLVRYYGVEVHREEvyIFM--EYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAK--------PKGNK 161
Cdd:cd06626   82 QEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVklknntttMAPGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQtccGSLAYAAPELIQGKSYLGSE--ADVWSMGILLYVLMCGFLPFDD-DNVMAL-YKKIMRGKYDVPK--WLSPS 235
Cdd:cd06626  161 VNSLV---GTPAYMAPEVITGNKGEGHGraADIWSLGCVVLEMATGKRPWSElDNEWAImYHVGMGHKPPIPDslQLSPE 237
                        250       260
                 ....*....|....*....|....*...
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06626  238 GKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
11-263 3.07e-41

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: 150.01  E-value: 3.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD-----LPRiktEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvqkfLPR---ELSILRRVNHPNIVQMFECIEVANGRLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKGNKDYH 164
Cdd:cd14164   79 VMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYPELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVmalykKIMRGKYDVPKWLSPSSIL-----L 239
Cdd:cd14164  159 -TTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNV-----RRLRLQQRGVLYPSGVALEepcraL 232
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14164  233 IRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
11-285 3.90e-41

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: 152.08  E-value: 3.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD----LPRIKTEIEALKNlrHQHICQLYHVLETANKIFMVL 86
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQeevsFFEEERDIMAKAN--SPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHL 165
Cdd:cd05601   81 EYHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQ-----GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK----YDVPKWLSPSS 236
Cdd:cd05601  161 KMPVGTPDYIAPEVLTsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkflkFPEDPKVSESA 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 237 ILLLQQMLQvDPKKRISMKNLLNHPWIMQdynypVEW----QSKNPF---IHLDDD 285
Cdd:cd05601  241 VDLIKGLLT-DAKERLGYEGLCCHPFFSG-----IDWnnlrQTVPPFvptLTSDDD 290
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
15-262 5.59e-41

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: 149.49  E-value: 5.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP-RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCpGGE 93
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQEsQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL-HGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKPKGNKDYHlQTC 168
Cdd:cd14082   88 MLEMILSSEkgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLasaEPFPQVKLCDFGF-ARIIGEKSFR-RSV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNvmALYKKIMRGKYDVP----KWLSPSSILLLQQML 244
Cdd:cd14082  166 VGTPAYLAPEVLRNKGYNRS-LDMWSVGVIIYVSLSGTFPFNEDE--DINDQIQNAAFMYPpnpwKEISPDAIDLINNLL 242
                        250
                 ....*....|....*...
gi 375493532 245 QVDPKKRISMKNLLNHPW 262
Cdd:cd14082  243 QVKMRKRYSVDKSLSHPW 260
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
11-263 7.30e-41

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: 149.63  E-value: 7.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyhlQTC 168
Cdd:cd14117   88 APRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRR---RTM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd14117  165 CGTLDYLPPEMIEGRTH-DEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                        250
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14117  244 SERLPLKGVMEHPWV 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
10-263 9.50e-41

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 148.51  E-value: 9.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLR--KQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDyIISQ--DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKdyh 164
Cdd:cd06614   79 DGGSLTD-IITQnpVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAqltKEKSKR--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLP-FDDDNVMALY----KKIMRGKYdvPKWLSPSSILL 239
Cdd:cd06614  155 -NSVVGTPYWMAPEVIKRKDY-GPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFlittKGIPPLKN--PEKWSPEFKDF 230
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06614  231 LNKCLVKDPEKRPSAEELLQHPFL 254
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
11-282 9.73e-41

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: 149.78  E-value: 9.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSdlpriKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDP-----SEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-DEY---HKLKLIDFGLCAKPKGNKDYhL 165
Cdd:cd14177   81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmDDSanaDSIRICDFGFAKQLRGENGL-L 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF---DDDNVMALYKKIMRGKYDVP--KW--LSPSSIL 238
Cdd:cd14177  160 LTPCYTANFVAPEVLMRQGY-DAACDIWSLGVLLYTMLAGYTPFangPNDTPEEILLRIGSGKFSLSggNWdtVSDAAKD 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHL 282
Cdd:cd14177  239 LLSHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHL 282
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
11-263 1.47e-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. 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: 148.78  E-value: 1.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKI--MDKNTLGsdLP----RiktEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKirLDNEEEG--IPstalR---EISLLKELKHPNIVKLLDVIHTENKLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGgELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAK----PKG 159
Cdd:cd07829   76 VFEYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGL-ARafgiPLR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTccgsLAYAAPELIQGKSYLGSEADVWSMGILLY------VLMCGflpfdDDNVMALYK--KIM--------- 222
Cdd:cd07829  154 TYTHEVVT----LWYRAPEILLGSKHYSTAVDIWSVGCIFAelitgkPLFPG-----DSEIDQLFKifQILgtpteeswp 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 223 ------RGKYDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07829  225 gvtklpDYKPTFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
17-262 1.69e-40

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: 150.06  E-value: 1.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALkNLRHQH--ICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVIlqDDDVECTMTEKRIL-SLARNHpfLTQLYCCFQTPDRLFFVMEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05590   82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMC-KEGIFNGKTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05590  161 DYIAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRL 239
                        250
                 ....*....|....*.
gi 375493532 253 SM------KNLLNHPW 262
Cdd:cd05590  240 GSltlggeEAILRHPF 255
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
17-273 2.16e-40

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: 149.84  E-value: 2.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIE----ALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIErrvlALAS-QHPFLTHLFCTFQTESHLFFVMEYLNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05592   82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC-KENIYGENKASTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05592  161 DYIAPEILKGQKY-NQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRL 239
                        250       260
                 ....*....|....*....|.
gi 375493532 253 SMKNLLNHPWIMQDYNYPVEW 273
Cdd:cd05592  240 GVPECPAGDIRDHPFFKTIDW 260
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
11-263 2.58e-40

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: 148.56  E-value: 2.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-------------GSD------------LPRIKTEIEALKNLR 65
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprGSKaaqgeqakplapLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  66 HQHICQLYHVLE--TANKIFMVLEYCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY 143
Cdd:cd14200   82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 144 HKLKLIDFGLCAKPKGNkDYHLQTCCGSLAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKI 221
Cdd:cd14200  161 GHVKIADFGVSNQFEGN-DALLSSTAGTPAFMAPETLsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 222 MRGKYDVPKWLSPSSIL--LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14200  240 KNKPVEFPEEPEISEELkdLILKMLDKNPETRITVPEIKVHPWV 283
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-263 2.76e-40

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: 147.81  E-value: 2.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14113    9 YSEVAE-LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRD--QVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKPkgNKDYHLQ 166
Cdd:cd14113   86 DQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQL--NTTYYIH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP----KWLSPSSILLLQQ 242
Cdd:cd14113  164 QLLGSPEFAAPEIILGNP-VSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCF 242
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14113  243 LLQMDPAKRPSAALCLQEQWL 263
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-252 3.04e-40

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: 150.23  E-value: 3.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   1 MKDYDELlkyyelhETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLET 78
Cdd:cd05593   14 MNDFDYL-------KLLGKGTFGKVILVREKASGKYYAMKILKKEVIiaKDEVAHTLTESRVLKNTRHPFLTSLKYSFQT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPK 158
Cdd:cd05593   87 KDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC-KEG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSIL 238
Cdd:cd05593  166 ITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKS 244
                        250
                 ....*....|....
gi 375493532 239 LLQQMLQVDPKKRI 252
Cdd:cd05593  245 LLSGLLIKDPNKRL 258
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
11-274 3.24e-40

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: 150.18  E-value: 3.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvaKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFdYIISQDRL-SEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkGNKD-YHL 165
Cdd:cd05594  107 ANGGELF-FHLSRERVfSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKE--GIKDgATM 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd05594  184 KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLK 262
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 246 VDPKKRI-----SMKNLLNHPWIMQdynypVEWQ 274
Cdd:cd05594  263 KDPKQRLgggpdDAKEIMQHKFFAG-----IVWQ 291
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
17-267 3.56e-40

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: 3.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIK--TEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKmsMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCCGSLAY 174
Cdd:cd14187   95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERK-KTLCGTPNY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISM 254
Cdd:cd14187  174 IAPEVLSKKGH-SFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTI 252
                        250
                 ....*....|...
gi 375493532 255 KNLLNHPWIMQDY 267
Cdd:cd14187  253 NELLNDEFFTSGY 265
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-263 8.78e-40

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: 147.22  E-value: 8.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMdkntlgsdLPRIKTEIEALKNLR---HQHICQLYHV----------LETANK 81
Cdd:cd14171   12 QKLGTGISGPVRVCVKKSTGERFALKIL--------LDRPKARTEVRLHMMcsgHPNIVQIYDVyansvqfpgeSSPRAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLCAKPK 158
Cdd:cd14171   84 LLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKVDQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNkdyhLQTCCGSLAYAAPELIQGKSYLGSE----------------ADVWSMGILLYVLMCGFLPFDD-------DNVM 215
Cdd:cd14171  164 GD----LMTPQFTPYYVAPQVLEAQRRHRKErsgiptsptpytydksCDMWSLGVIIYIMLCGYPPFYSehpsrtiTKDM 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 216 AlyKKIMRGKYDVP----KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14171  240 K--RKIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-262 9.93e-40

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: 148.14  E-value: 9.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKV----KLACHIlTGEMVAIKIMDKNTL---GSDLPRIKTEIEALKNLRHQ-HICQLYHVLETANKI 82
Cdd:cd05614    2 FELLKVLGTGAYGKVflvrKVSGHD-ANKLYAMKVLRKAALvqkAKTVEHTRTERNVLEHVRQSpFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD 162
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFD---DDNVMA-LYKKIMRGKYDVPKWLSPSSIL 238
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTlegEKNTQSeVSRRILKCDPPFPSFIGPVARD 240
                        250       260
                 ....*....|....*....|....*....
gi 375493532 239 LLQQMLQVDPKKRI-----SMKNLLNHPW 262
Cdd:cd05614  241 LLQKLLCKDPKKRLgagpqGAQEIKEHPF 269
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
17-262 1.19e-39

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: 146.00  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKL---ACHILTGEMVAIKIMDKNTL---GSDLPRIKTEIEALKNLRHQ-HICQLYHVLETANKIFMVLEYC 89
Cdd:cd05583    2 LGTGAYGKVFLvrkVGGHDAGKLYAMKVLKKATIvqkAKTAEHTMTERQVLEAVRQSpFLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd05583   82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYLGSEA-DVWSMGILLYVLMCGFLPF---DDDNVMA-LYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd05583  162 GTIEYMAPEVVRGGSDGHDKAvDWWSLGVLTYELLTGASPFtvdGERNSQSeISKRILKSHPPIPKTFSAEAKDFILKLL 241
                        250       260
                 ....*....|....*....|...
gi 375493532 245 QVDPKKRI-----SMKNLLNHPW 262
Cdd:cd05583  242 EKDPKKRLgagprGAHEIKEHPF 264
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
17-273 1.31e-39

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: 147.42  E-value: 1.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEAL-KNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTIlkKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKdyhlQTCCG 170
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKegmEPEETT----STFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd05603  159 TPEYLAPEVLRKEPY-DRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRR 237
                        250       260
                 ....*....|....*....|....*..
gi 375493532 251 RISMK----NLLNHPWIMqdynyPVEW 273
Cdd:cd05603  238 RLGAKadflEIKNHVFFS-----PINW 259
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
17-262 1.33e-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: 147.80  E-value: 1.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpRIKTEIEA-----LKNLRHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNR--KEQKHIMAernvlLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLqTCCGS 171
Cdd:cd05604   82 GELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTT-TFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd05604  161 PEYLAPEVIRKQPY-DNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLR 239
                        250
                 ....*....|....*
gi 375493532 252 ISMKN----LLNHPW 262
Cdd:cd05604  240 LGAKEdfleIKNHPF 254
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
11-261 1.51e-39

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: 145.25  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRkMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQT 167
Cdd:cd08529   82 ENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGV-AKILSDTTNFAQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSSILLLQQMLQV 246
Cdd:cd08529  161 IVGTPYYLSPELCEDKPY-NEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLTK 239
                        250
                 ....*....|....*
gi 375493532 247 DPKKRISMKNLLNHP 261
Cdd:cd08529  240 DYRQRPDTTELLRNP 254
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
17-263 1.52e-39

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: 145.58  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR----IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKevkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnkdyhLQTCC--- 169
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKR--------LQTICsst 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 ------GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM--RGKYDVPKWLSPSSILLLQ 241
Cdd:cd06625  160 gmksvtGTPYWMSPEVINGEGY-GRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtqPTNPQLPPHVSEDARDFLS 238
                        250       260
                 ....*....|....*....|..
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06625  239 LIFVRNKKQRPSAEELLSHSFV 260
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
17-280 2.17e-39

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: 146.78  E-value: 2.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHIL---TGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05582    3 LGQGSFGKVFLVRKITgpdAGTLYAMKVLKKATLKvRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKP--KGNKDYHLqtcCG 170
Cdd:cd05582   83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESidHEKKAYSF---CG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd05582  160 TVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPAN 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 375493532 251 RI-----SMKNLLNHPWIMQ-DYNYPVEWQSKNPFI 280
Cdd:cd05582  239 RLgagpdGVEEIKRHPFFATiDWNKLYRKEIKPPFK 274
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
11-262 3.19e-39

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: 144.74  E-value: 3.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14010    2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDK----SKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDyIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL---------------C 154
Cdd:cd14010   78 GGDLET-LLRQDgNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLarregeilkelfgqfS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQTCCGSLAYAAPELIQGKSYlgSEA-DVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKW-- 231
Cdd:cd14010  157 DEGNVNKVSKKQAKRGTPYYMAPELFQGGVH--SFAsDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPkv 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 232 ---LSPSSILLLQQMLQVDPKKRISMKNLLNHP-W 262
Cdd:cd14010  235 sskPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
11-263 5.58e-39

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: 145.38  E-value: 5.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL----GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFtsspGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGEL-FDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLcAKPKG 159
Cdd:cd14094   85 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV-AIQLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 nkDYHLQTC--CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVmALYKKIMRGKYDV--PKW--LS 233
Cdd:cd14094  164 --ESGLVAGgrVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnpRQWshIS 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14094  240 ESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
11-263 5.76e-39

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: 143.95  E-value: 5.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE---DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCC 169
Cdd:cd06612   82 AGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKR-NTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd06612  161 GTPFWMAPEVIQEIGY-NNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKpppTLSDPEKWSPEFNDFVKKCLVK 239
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd06612  240 DPEERPSAIQLLQHPFI 256
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
15-263 8.14e-39

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: 143.31  E-value: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIK---IMDKNTLGSD-LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSREsVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyHLQTCCG 170
Cdd:cd06632   86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFS--FAKSFKG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELI--QGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY--DVPKWLSPSSILLLQQMLQV 246
Cdd:cd06632  164 SPYWMAPEVImqKNSGY-GLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQR 242
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd06632  243 DPEDRPTASQLLEHPFV 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-263 9.32e-39

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: 143.59  E-value: 9.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMdkntlgSDLPRIKTEIEA-LKNLRHQHICQLYHVLETANK----IFMVLEYC 89
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLL------YDSPKARREVEHhWRASGGPHIVHILDVYENMHHgkrcLLIIMECM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIisQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLcAKPKGNKD 162
Cdd:cd14172   84 EGGELFSRI--QERgdqaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKdavLKLTDFGF-AKETTVQN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 yHLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMA----LYKKIMRGKYDV--PKW--LSP 234
Cdd:cd14172  161 -ALQTPCYTPYYVAPEVLGPEKYDKS-CDMWSLGVIMYILLCGFPPFYSNTGQAispgMKRRIRMGQYGFpnPEWaeVSE 238
                        250       260
                 ....*....|....*....|....*....
gi 375493532 235 SSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14172  239 EAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
17-262 1.05e-38

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: 144.69  E-value: 1.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05574    9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMikRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQ--DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC------------------ 154
Cdd:cd05574   89 FRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSkqssvtpppvrkslrkgs 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQ----------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG 224
Cdd:cd05574  169 RRSSVKSIEKETfvaepsarsnSFVGTEEYIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKK 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 225 KYDVPKWLSPSSIL--LLQQMLQVDPKKRISMKN----LLNHPW 262
Cdd:cd05574  248 ELTFPESPPVSSEAkdLIRKLLVKDPSKRLGSKRgaseIKRHPF 291
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-263 1.61e-38

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: 142.42  E-value: 1.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS--DLP---RIKTEIEALKNLRH--QHICQLYHVLETANKIF 83
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwgELPngtRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYC-PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKGN- 160
Cdd:cd14100   82 LVLERPePVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDTv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 -KDYHlqtccGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDnvmalyKKIMRGKYDVPKWLSPSSILL 239
Cdd:cd14100  162 yTDFD-----GTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHD------EEIIRGQVFFRQRVSSECQHL 230
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14100  231 IKWCLALRPSDRPSFEDIQNHPWM 254
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-269 1.72e-38

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: 143.60  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHIL---TGEMVAIKIMDKNTL---GSDLPRIKTEIEALKNLRHQ-HICQLYHVLETANKIF 83
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIvqkAKTAEHTRTERQVLEHIRQSpFLVTLHYAFQTDTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd05613   82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYLGSEA-DVWSMGILLYVLMCGFLPF----DDDNVMALYKKIMRGKYDVPKWLSPSSIL 238
Cdd:cd05613  162 RAYSFCGTIEYMAPEIVRGGDSGHDKAvDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKD 241
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 375493532 239 LLQQMLQVDPKKRI-----SMKNLLNHPWiMQDYNY 269
Cdd:cd05613  242 IIQRLLMKDPKKRLgcgpnGADEIKKHPF-FQKINW 276
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-264 6.82e-38

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: 140.75  E-value: 6.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG--SDLPRIKT---EIEALKNL----RHQHICQLYHVLETANK 81
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQqwSKLPGVNPvpnEVALLQSVgggpGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEY-CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKG 159
Cdd:cd14101   82 FLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATLKD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 N--KDYHlqtccGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDnvmalyKKIMRGKYDVPKWLSPSSI 237
Cdd:cd14101  162 SmyTDFD-----GTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERD------TDILKAKPSFNKRVSNDCR 230
                        250       260
                 ....*....|....*....|....*..
gi 375493532 238 LLLQQMLQVDPKKRISMKNLLNHPWIM 264
Cdd:cd14101  231 SLIRSCLAYNPSDRPSLEQILLHPWMM 257
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
66-263 1.17e-37

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: 139.63  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  66 HQHICQLYHVLETANKIFMVLEYcPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK 145
Cdd:cd14024   44 HEGVCSVLEVVIGQDRAYAFFSR-HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 146 LKLIDFGL--CAKPKGNKDyHLQTCCGSLAYAAPELIQ-GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM 222
Cdd:cd14024  123 TKLVLVNLedSCPLNGDDD-SLTDKHGCPAYVGPEILSsRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIR 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 375493532 223 RGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14024  202 RGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
9-261 1.37e-37

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: 140.43  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLA----CHILtgemvAIKIMD-KNTLGSDLPRIKTEIEALKNLRHQ-HICQL--YHVLETAN 80
Cdd:cd14131    1 KPYEILKQLGKGGSSKVYKVlnpkKKIY-----ALKRVDlEGADEQTLQSYKNEIELLKKLKGSdRIIQLydYEVTDEDD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYcpgGEL-FDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEyHKLKLIDFGLcAK 156
Cdd:cd14131   76 YLYMVMEC---GEIdLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGI-AK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 --PKGNKDYHLQTCCGSLAYAAPELIQGKSY---------LGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRG 224
Cdd:cd14131  151 aiQNDTTSIVRDSQVGTLNYMSPEAIKDTSAsgegkpkskIGRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAIIDP 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 375493532 225 KYDV--PKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14131  231 NHEIefPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
15-263 2.23e-37

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: 139.82  E-value: 2.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKI--MDKNTLGSDLPR-------IKTEIEALKNLRHQHICQlYHVLETANKIFMV 85
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQveLPKTSSDRADSRqktvvdaLKSEIDTLKDLDHPNIVQ-YLGFEETEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 -LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYH 164
Cdd:cd06629   86 fLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYGNN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCC-GSLAYAAPELI--QGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM--RGKYDVPK--WLSPSSI 237
Cdd:cd06629  166 GATSMqGSVFWMAPEVIhsQGQGY-SAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGnkRSAPPVPEdvNLSPEAL 244
                        250       260
                 ....*....|....*....|....*.
gi 375493532 238 LLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06629  245 DFLNACFAIDPRDRPTAAELLSHPFL 270
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
12-258 2.75e-37

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 139.20  E-value: 2.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    12 ELHETIGTGGFAKVKLACHIL----TGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGkggkKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    88 YCPGGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:smart00219  82 YMEGGDLLSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL-SRDLYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   167 TCCGS-LAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLLQQM 243
Cdd:smart00219 161 RGGKLpIRWMAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNGYRlPQPPNCPPELYDLMLQC 239
                          250
                   ....*....|....*
gi 375493532   244 LQVDPKKRISMKNLL 258
Cdd:smart00219 240 WAEDPEDRPTFSELV 254
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
17-262 2.86e-37

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: 139.00  E-value: 2.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKImdkntlgsdLPRIKTEIEALknLR----------HQHICQLYHV-LETANKIFMV 85
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKF---------VPKPSTKLKDF--LReynislelsvHPHIIKTYDVaFETEDYYVFA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPEN-LLFD-EYHKLKLIDFGLCAKpkgnKDY 163
Cdd:cd13987   70 QEYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDkDCRRVKLCDFGLTRR----VGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYLGSEA----DVWSMGILLYVLMCGFLPF----DDDNVMALYKKIMRGK-YDVP-KW-- 231
Cdd:cd13987  146 TVKRVSGTIPYTAPEVCEAKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWekadSDDQFYEEFVRWQKRKnTAVPsQWrr 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 232 LSPSSILLLQQMLQVDPKKRISMKNL---LNHPW 262
Cdd:cd13987  226 FTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
9-263 2.87e-37

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: 139.19  E-value: 2.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14111    3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQ--GVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG-------LCAKPKGNK 161
Cdd:cd14111   81 CSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaqsfnpLSLRQLGRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 dyhlqtcCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKW---LSPSSIL 238
Cdd:cd14111  161 -------TGTLEYMAPEMVKGEP-VGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLypnVSQSASL 232
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14111  233 FLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
11-263 3.10e-37

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: 138.98  E-value: 3.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVI-KLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-----PKGNkdyhl 165
Cdd:cd06613   81 GGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQltatiAKRK----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 qTCCGSLAYAAPELIQGKSYLG--SEADVWSMGILLYVLMCGFLP-FDDDNVMALYkKIMRGKYDVP------KWlSPSS 236
Cdd:cd06613  156 -SFIGTPYWMAPEVAAVERKGGydGKCDIWALGITAIELAELQPPmFDLHPMRALF-LIPKSNFDPPklkdkeKW-SPDF 232
                        250       260
                 ....*....|....*....|....*..
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06613  233 HDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7-263 3.59e-37

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: 140.39  E-value: 3.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYEL---HETIGTGGFAKVKLACHILTGEMVAIKI----MDKNTlgsdlpriKTEIEALKNLR-HQHICQLYHVLET 78
Cdd:cd14180    1 FFQCYELdleEPALGEGSFSVCRKCRHRQSGQEYAVKIisrrMEANT--------QREVAALRLCQsHPNIVALHEVLHD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLCA 155
Cdd:cd14180   73 QYHTYLVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 -KPKGNKDyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFD-------DDNVMALYKKIMRGKYD 227
Cdd:cd14180  153 lRPQGSRP--LQTPCFTLQYAAPELFSNQGYDES-CDLWSLGVILYTMLSGQVPFQskrgkmfHNHAADIMHKIKEGDFS 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 375493532 228 VP----KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14180  230 LEgeawKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWL 269
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
17-263 5.41e-37

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: 138.82  E-value: 5.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--------LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGN-----KDY 163
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANslstkNNG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDVPKWLSPSSILLLQQ 242
Cdd:cd06628  168 ARPSLQGSVFWMAPEVVKQTSY-TRKADIWSLGCLVVEMLTGTHPFPDCTQMqAIFKIGENASPTIPSNISSEARDFLEK 246
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06628  247 TFEIDHNKRPTADELLKHPFL 267
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
8-263 5.51e-37

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: 139.33  E-value: 5.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPR-----------------------IKTEIEALK 62
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrQAGFPRrppprgaraapegctqprgpierVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  63 NLRHQHICQLYHVLETANK--IFMVLEYCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF 140
Cdd:cd14199   81 KLDHPNVVKLVEVLDDPSEdhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 141 DEYHKLKLIDFGLCAKPKGNkDYHLQTCCGSLAYAAPELIQG--KSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALY 218
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGS-DALLTNTVGTPAFMAPETLSEtrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 219 KKIMRGKYDVPKWLSPSSIL--LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14199  239 SKIKTQPLEFPDQPDISDDLkdLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-222 1.08e-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: 140.20  E-value: 1.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05596   28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMikRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05596  108 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLVRSDTA 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 169 CGSLAYAAPELIQ---GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM 222
Cdd:cd05596  187 VGTPDYISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIM 243
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
11-263 1.94e-36

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: 137.57  E-value: 1.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06611    7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIES-EEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCC 169
Cdd:cd06611   86 GGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKR-DTFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSY----LGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGkyDVPKWLSPSSIL-----LL 240
Cdd:cd06611  165 GTPYWMAPEVVACETFkdnpYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKS--EPPTLDQPSKWSssfndFL 242
                        250       260
                 ....*....|....*....|...
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06611  243 KSCLVKDPDDRPTAAELLKHPFV 265
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
11-263 2.41e-36

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: 136.59  E-value: 2.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELH--ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14190    4 FSIHskEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQN-SKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDyhL 165
Cdd:cd14190   83 VEGGELFERIVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREK--L 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY----DVPKWLSPSSILLLQ 241
Cdd:cd14190  161 KVNFGTPEFLSPEVVN-YDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWyfdeETFEHVSDEAKDFVS 239
                        250       260
                 ....*....|....*....|..
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14190  240 NLIIKERSARMSATQCLKHPWL 261
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
11-262 2.87e-36

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: 137.28  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGS--DLPRIKtEIEALKNL-RHQHICQLYHVLETANKIFMVLE 87
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-KKKFYSweECMNLR-EVKSLRKLnEHPNIVKLKEVFRENDELYFVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGgELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNK---- 161
Cdd:cd07830   79 YMEG-NLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGL-AREIRSRppyt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYhlqtcCGSLAYAAPELIQGKSYLGSEADVWSMG-IL--LYVL---------------MCGFL----PFDDDNVMALYK 219
Cdd:cd07830  157 DY-----VSTRWYRAPEILLRSTSYSSPVDIWALGcIMaeLYTLrplfpgsseidqlykICSVLgtptKQDWPEGYKLAS 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 220 KI-MRGKYDVPKWL-------SPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07830  232 KLgFRFPQFAPTSLhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-270 4.80e-36

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: 137.09  E-value: 4.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMdkntlgSDLPRIKTEIEA-LKNLRHQHICQLYHVLETANK----IFM 84
Cdd:cd14170    3 YKVTSQVLGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELhWRASQCPHIVRIVDVYENLYAgrkcLLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIisQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCAKP 157
Cdd:cd14170   77 VMECLDGGELFSRI--QDRgdqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFAKET 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKDyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMA----LYKKIMRGKYDVP--KW 231
Cdd:cd14170  155 TSHNS--LTTPCYTPYYVAPEVLGPEKYDKS-CDMWSLGVIMYILLCGYPPFYSNHGLAispgMKTRIRMGQYEFPnpEW 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 375493532 232 --LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYP 270
Cdd:cd14170  232 seVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVP 272
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
11-262 5.02e-36

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: 136.69  E-value: 5.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP----RiktEIEALKNLR-HQHICQLYHVLETANKIFMV 85
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPnqalR---EIKALQACQgHPYVVKLRDVFPHGTGFVLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGeLFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA--KPKGNKD 162
Cdd:cd07832   79 FEYMLSS-LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARlfSEEDPRL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQtcCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMA------------------------LY 218
Cdd:cd07832  158 YSHQ--VATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEqlaivlrtlgtpnektwpeltslpDY 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 219 KKI-------MRGKYDVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07832  236 NKItfpeskgIRLEEIFPD-CSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-263 6.99e-36

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: 135.08  E-value: 6.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKN------TLGSDLprIKTEIEALKNL--RHQHICQLYHVLETANKI 82
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKErvtewgTLNGVM--VPLEIVLLKKVgsGFRGVIKLLDWYERPDGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYC-PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKGN 160
Cdd:cd14102   80 LIVMERPePVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKDT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 --KDYHlqtccGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDnvmalyKKIMRGKYDVPKWLSPSSIL 238
Cdd:cd14102  160 vyTDFD-----GTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQD------EEILRGRLYFRRRVSPECQQ 228
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14102  229 LIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
10-263 7.43e-36

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: 135.13  E-value: 7.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14191    3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF-KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDyhLQ 166
Cdd:cd14191   82 SGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAGS--LK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP----KWLSPSSILLLQQ 242
Cdd:cd14191  160 VLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 238
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14191  239 LLKKDMKARLTCTQCLQHPWL 259
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
17-259 7.85e-36

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: 135.50  E-value: 7.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd13996   14 LGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTLRD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVV---FRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGL-------------CAKPKG 159
Cdd:cd13996   94 WIDRRNSSSKNDRKLAlelFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLatsignqkrelnnLNNNNN 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFlpfddDNVMALYKKI--MRgKYDVPKWLS---P 234
Cdd:cd13996  174 GNTSNNSVGIGTPLYASPEQLDGENY-NEKADIYSLGIILFEMLHPF-----KTAMERSTILtdLR-NGILPESFKakhP 246
                        250       260
                 ....*....|....*....|....*
gi 375493532 235 SSILLLQQMLQVDPKKRISMKNLLN 259
Cdd:cd13996  247 KEADLIQSLLSKNPEERPSAEQLLR 271
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
11-256 1.81e-35

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: 136.69  E-value: 1.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEAL-KNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAIlkKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKdyh 164
Cdd:cd05602   89 YINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKeniEPNGTT--- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQML 244
Cdd:cd05602  166 -STFCGTPEYLAPEVLHKQPY-DRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLL 243
                        250
                 ....*....|..
gi 375493532 245 QVDPKKRISMKN 256
Cdd:cd05602  244 QKDRTKRLGAKD 255
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
9-263 2.01e-35

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: 134.28  E-value: 2.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgSDLPR---IKTEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd06647    7 KKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNL----QQQPKkelIINEILVMRENKNPNIVNYLDSYLVGDELWVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDy 163
Cdd:cd06647   83 MEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitPEQSKR- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 hlQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDV--PKWLSPSSILLL 240
Cdd:cd06647  161 --STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGTPELqnPEKLSAIFRDFL 237
                        250       260
                 ....*....|....*....|...
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06647  238 NRCLEMDVEKRGSAKELLQHPFL 260
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
17-262 2.21e-35

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 133.55  E-value: 2.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD---EYHKLKLIDFGLCAKPKGNkdYHLQTCCGSLA 173
Cdd:cd14115   79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGH--RHVHHLLGNPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 174 YAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKW----LSPSSILLLQQMLQVDPK 249
Cdd:cd14115  157 FAAPEVIQGTP-VSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQEDPR 235
                        250
                 ....*....|...
gi 375493532 250 KRISMKNLLNHPW 262
Cdd:cd14115  236 RRPTAATCLQHPW 248
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
11-263 2.55e-35

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: 133.70  E-value: 2.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQaALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIisQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL-KLIDFG----LCAKPKGN 160
Cdd:cd08220   82 PGGTLFEYI--QQRkgslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGiskiLSSKSKAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 kdyhlqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSSILL 239
Cdd:cd08220  160 ------TVVGTPCYISPELCEGKPY-NQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHL 232
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd08220  233 ILSMLHLDPNKRPTLSEIMAQPII 256
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
12-259 3.42e-35

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: 133.44  E-value: 3.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    12 ELHETIGTGGFAKVKLA----CHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    88 YCPGGELFDYI-ISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHL 165
Cdd:smart00221  82 YMPGGDLLDYLrKNRPKELSLSDLLSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL-SRDLYDDDYYK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   166 QTCC-GSLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLLQQ 242
Cdd:smart00221 161 VKGGkLPIRWMAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKGYRlPKPPNCPPELYKLMLQ 239
                          250
                   ....*....|....*..
gi 375493532   243 MLQVDPKKRISMKNLLN 259
Cdd:smart00221 240 CWAEDPEDRPTFSELVE 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
11-262 5.63e-35

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: 133.60  E-value: 5.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKT-EIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALrEVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd07833   83 ERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTDYV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYLGSEADVWSMGIL-------------------LYVLM--CGFLP------FDDDNVMALYKKI- 221
Cdd:cd07833  163 ATRWYRAPELLVGDTNYGKPVDVWAIGCImaelldgeplfpgdsdidqLYLIQkcLGPLPpshqelFSSNPRFAGVAFPe 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 222 ------MRGKYdvPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07833  243 psqpesLERRY--PGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
28-262 5.67e-35

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: 132.47  E-value: 5.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  28 ACHILTGEMVAIKIMDkntlgsdLPRIKTEIEALKNL-RHQHICQLYHVL--ETANKIFMVLEYcpgGELFDYIISQDRL 104
Cdd:cd14022   12 AVHLHSGEELVCKVFD-------IGCYQESLAPCFCLpAHSNINQITEIIlgETKAYVFFERSY---GDMHSFVRTCKKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 105 SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDyHLQTCCGSLAYAAPELIQG 182
Cdd:cd14022   82 REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFkdEERTRVKLESLEDAYILRGHDD-SLSDKHGCPAYVSPEILNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 183 K-SYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14022  161 SgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 240

                 .
gi 375493532 262 W 262
Cdd:cd14022  241 W 241
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
12-260 7.83e-35

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 132.23  E-value: 7.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   12 ELHETIGTGGFAKVKLA----CHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   88 YCPGGELFDYIISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:pfam07714  82 YMPGGDLLDFLRKHKRKLTLKDLLSMaLQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGL-SRDIYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  167 TCCGSL--AYAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGKY-DVPKwLSPSSI-LLLQ 241
Cdd:pfam07714 161 RGGGKLpiKWMAPESLKDGKF-TSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLEDGYRlPQPE-NCPDELyDLMK 238
                         250
                  ....*....|....*....
gi 375493532  242 QMLQVDPKKRISMKNLLNH 260
Cdd:pfam07714 239 QCWAYDPEDRPTFSELVED 257
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
17-279 8.28e-35

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: 134.16  E-value: 8.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTE--IEALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVIlqDDDVDCTMTEkrILALAA-KHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05591   82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC-KEGILNGKTTTTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05591  161 DYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRL 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 253 SM-------KNLLNHPWIMQ-DYNYPVEWQSKNPF 279
Cdd:cd05591  240 GCvasqggeDAIRQHPFFREiDWEALEQRKVKPPF 274
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
11-261 8.78e-35

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: 133.40  E-value: 8.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlgsdlPRIKT-EIEALKNLRHQHICQL----YHVLETANKIF-- 83
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQD------KRYKNrELQIMRRLKHPNIVKLkyffYSSGEKKDEVYln 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGgELFDYIIS----QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGlCAKP- 157
Cdd:cd14137   80 LVMEYMPE-TLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFG-SAKRl 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 -KG--NKDYHlqtccGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPF---DDDNVMALYKKI---------- 221
Cdd:cd14137  158 vPGepNVSYI-----CSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFpgeSSVDQLVEIIKVlgtptreqik 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 222 -MRGKYDV---------------PKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14137  233 aMNPNYTEfkfpqikphpwekvfPKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
17-262 1.55e-34

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 131.83  E-value: 1.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS--DLPRIKTEIEALKNLRHQ-HICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAknQVTNVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKDYhlqtcCG 170
Cdd:cd05611   84 CASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRnglEKRHNKKF-----VG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSylGSEA-DVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK----WLSPSSILLLQQMLQ 245
Cdd:cd05611  159 TPDYLAPETILGVG--DDKMsDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLC 236
                        250       260
                 ....*....|....*....|
gi 375493532 246 VDPKKRISMK---NLLNHPW 262
Cdd:cd05611  237 MDPAKRLGANgyqEIKSHPF 256
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
10-263 2.14e-34

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: 131.24  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYEL--HETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14192    3 YYAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKII-KVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY--HKLKLIDFGLCAKPKGNKDyh 164
Cdd:cd14192   82 YVDGGELFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLARRYKPREK-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP----KWLSPSSILLL 240
Cdd:cd14192  160 LKVNFGTPEFLAPEVVN-YDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFI 238
                        250       260
                 ....*....|....*....|...
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14192  239 SRLLVKEKSCRMSATQCLKHEWL 261
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
17-263 3.54e-34

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: 130.64  E-value: 3.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDkntLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMD---LRKQQRRelLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGAL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-----PKgnkdyhLQTCC 169
Cdd:cd06648   92 TD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQvskevPR------RKSLV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKWLSPSSILLLQQMLQV 246
Cdd:cd06648  165 GTPYWMAPEVISRLPY-GTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNeppKLKNLHKVSPRLRSFLDRMLVR 243
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd06648  244 DPAQRATAAELLNHPFL 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
11-262 4.79e-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: 130.87  E-value: 4.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-I-MDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKkIrLETEDEGVPSTAIR-EISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CpGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAK----PKGNKD 162
Cdd:cd07835   80 L-DLDLKKYMdsSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGL-ARafgvPVRTYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTccgsLAYAAPELIQGKSYLGSEADVWSMG------ILLYVLMCGFLPFD------------DDNVMALYKKIMRG 224
Cdd:cd07835  158 HEVVT----LWYRAPEILLGSKHYSTPVDIWSVGcifaemVTRRPLFPGDSEIDqlfrifrtlgtpDEDVWPGVTSLPDY 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 225 KYDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07835  234 KPTFPKWarqdlskvvpsLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-225 5.89e-34

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: 133.20  E-value: 5.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05621   54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05621  134 MPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCDTA 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQ---GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd05621  213 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHK 272
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
11-261 6.03e-34

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 129.82  E-value: 6.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgSDLPRIKT--EIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSL-SQKEREDSvnEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyh 164
Cdd:cd08530   81 APFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNL--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSSILLLQQM 243
Cdd:cd08530  158 AKTQIGTPLYAAPEVWKGRPY-DYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPpIPPVYSQDLQQIIRSL 236
                        250
                 ....*....|....*...
gi 375493532 244 LQVDPKKRISMKNLLNHP 261
Cdd:cd08530  237 LQVNPKKRPSCDKLLQSP 254
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
66-262 7.11e-34

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: 129.40  E-value: 7.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  66 HQHICQLYHVLETANKIFMVLEYcPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEY 143
Cdd:cd14023   44 HRNITGIVEVILGDTKAYVFFEK-DFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsdEER 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 144 HKLKLIDFGLCAKPKGNKDyHLQTCCGSLAYAAPELIQGK-SYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM 222
Cdd:cd14023  123 TQLRLESLEDTHIMKGEDD-ALSDKHGCPAYVSPEILNTTgTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 375493532 223 RGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14023  202 RGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
11-262 1.03e-33

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: 129.99  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK--IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVL------ETANKI 82
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkiRMENEKEGFPITAIR-EIKLLQKLDHPNVVRLKEIVtskgsaKYKGSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPggelFDY--IISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL--CAK 156
Cdd:cd07840   80 YMVFEYMD----HDLtgLLDNPevKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLarPYT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDY--HLQTccgsLAYAAPELIQGKSYLGSEADVWSMGILLYVL---------------------MCGFlPFDDD- 212
Cdd:cd07840  156 KENNADYtnRVIT----LWYRPPELLLGATRYGPEVDMWSVGCILAELftgkpifqgkteleqlekifeLCGS-PTEENw 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375493532 213 -NVMAL-----------YKKIMRGKYDvpKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07840  231 pGVSDLpwfenlkpkkpYKRRLREVFK--NVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
17-261 1.08e-33

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: 129.04  E-value: 1.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVKkSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIIS---QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-PKGNKDYHlqtccG 170
Cdd:cd13997   88 QDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRlETSGDVEE-----G 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGF-LPFDDDnvmaLYKKIMRGKYDVPKWLSPSSIL--LLQQMLQVD 247
Cdd:cd13997  163 DSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEpLPRNGQ----QWQQLRQGKLPLPPGLVLSQELtrLLKVMLDPD 238
                        250
                 ....*....|....
gi 375493532 248 PKKRISMKNLLNHP 261
Cdd:cd13997  239 PTRRPTADQLLAHD 252
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
28-263 1.69e-33

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: 128.31  E-value: 1.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  28 ACHILTGEMVAIKIMDKNTLGSDL-PRIKTEiealknlRHQHICQLYHVLETANKIFMVLEYcPGGELFDYIISQDRLSE 106
Cdd:cd13976   12 CVDIHTGEELVCKVVPVPECHAVLrAYFRLP-------SHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLRE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 107 EETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDYhLQTCCGSLAYAAPELIQ-GK 183
Cdd:cd13976   84 PEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFadEERTKLRLESLEDAVILEGEDDS-LSDKHGCPAYVSPEILNsGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 184 SYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd13976  163 TYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-225 1.76e-33

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: 132.44  E-value: 1.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05622   75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMikRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05622  155 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTA 233
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQ---GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd05622  234 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK 293
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
10-263 1.76e-33

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: 128.88  E-value: 1.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHET--IGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14193    3 YYNVNKEeiLGGGRFGQVHKCEEKSSGLKLAAKII-KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKdyH 164
Cdd:cd14193   82 YVDGGELFDRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPRE--K 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPF--DDDNvmALYKKIMRGKYDVP----KWLSPSSIL 238
Cdd:cd14193  160 LRVNFGTPEFLAPEVVN-YEFVSFPTDMWSLGVIAYMLLSGLSPFlgEDDN--ETLNNILACQWDFEdeefADISEEAKD 236
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14193  237 FISKLLIKEKSWRMSASEALKHPWL 261
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
11-263 1.97e-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: 128.90  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyHLQTCCG 170
Cdd:cd06609   83 GGSVLDLLKPG-PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMS-KRNTFVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDdnvmalyKKIMRGKYDVPKwLSPSSILL----------L 240
Cdd:cd06609  161 TPFWMAPEVIKQSGY-DEKADIWSLGITAIELAKGEPPLSD-------LHPMRVLFLIPK-NNPPSLEGnkfskpfkdfV 231
                        250       260
                 ....*....|....*....|...
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06609  232 ELCLNKDPKERPSAKELLKHKFI 254
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
15-262 2.28e-33

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: 129.16  E-value: 2.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKI--MDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEYCpGG 92
Cdd:cd07860    6 EKIGEGTYGVVYKARNKLTGEVVALKKirLDTETEGVPSTAIR-EISLLKELNHPNIVKLLDVIHTENKLYLVFEFL-HQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDY--IISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG--NKDYHLQTC 168
Cdd:cd07860   84 DLKKFmdASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGL-ARAFGvpVRTYTHEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 cgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG------------------KYDVPK 230
Cdd:cd07860  163 --TLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTlgtpdevvwpgvtsmpdyKPSFPK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 375493532 231 W-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07860  241 WarqdfskvvppLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
15-262 5.13e-33

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: 128.91  E-value: 5.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD----LPRIKTEIEALKnLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDddveCTMVEKRVLALA-WENPFLTHLYCTFQTKEHLFFVMEFLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIisQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTC 168
Cdd:cd05620   80 GGDLMFHI--QDKGRFDLYRATFyaAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC-KENVFGDNRASTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd05620  157 CGTPDYIAPEILQGLKYTFS-VDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDP 235
                        250
                 ....*....|....*
gi 375493532 249 KKRISMK-NLLNHPW 262
Cdd:cd05620  236 TRRLGVVgNIRGHPF 250
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
10-265 5.56e-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: 5.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDkntLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06659   22 LLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMD---LRKQQRRelLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLME 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPkgNKDY-HLQ 166
Cdd:cd06659   99 YLQGGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI--SKDVpKRK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILL---LQQM 243
Cdd:cd06659  176 SLVGTPYWMAPEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLrdfLERM 254
                        250       260
                 ....*....|....*....|..
gi 375493532 244 LQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06659  255 LVRDPQERATAQELLDHPFLLQ 276
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
8-252 6.99e-33

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: 129.77  E-value: 6.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG--SDLPRIKTEIEALKNLR-HQHICQLYHVLETANKIFM 84
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNddEDIDWVQTEKHVFEQASnHPFLVGLHSCFQTESRLFF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYh 164
Cdd:cd05618   99 VIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD--------DDNVMA-LYKKIMRGKYDVPKWLSPS 235
Cdd:cd05618  178 TSTFCGTPNYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFDivgssdnpDQNTEDyLFQVILEKQIRIPRSLSVK 256
                        250
                 ....*....|....*..
gi 375493532 236 SILLLQQMLQVDPKKRI 252
Cdd:cd05618  257 AASVLKSFLNKDPKERL 273
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
17-263 7.34e-33

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: 127.36  E-value: 7.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDL-PRIKTEIEALKNLR-HQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCrMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIIS--QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL---KLIDFGLCAKPKGNKDyhLQTCC 169
Cdd:cd14197   97 FNQCVAdrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgdiKIVDFGLSRILKNSEE--LREIM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIqgkSY--LGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYDVPKW--LSPSSILLLQQM 243
Cdd:cd14197  175 GTPEYVAPEIL---SYepISTATDMWSIGVLAYVMLTGISPFlgDDKQETFLNISQMNVSYSEEEFehLSESAIDFIKTL 251
                        250       260
                 ....*....|....*....|
gi 375493532 244 LQVDPKKRISMKNLLNHPWI 263
Cdd:cd14197  252 LIKKPENRATAEDCLKHPWL 271
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
17-285 7.70e-33

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: 130.15  E-value: 7.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLfkLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGDF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-------------AKPKGNK 161
Cdd:cd05600   99 RTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAsgtlspkkiesmkIRLEEVK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHL-----------------------QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALY 218
Cdd:cd05600  179 NTAFleltakerrniyramrkedqnyaNSVVGSPDYMAPEVLRGEGY-DLTVDYWSLGCILFECLVGFPPFSGSTPNETW 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 219 -------KKIMRGKYDVPKW---LSPSSILLLQQMLqVDPKKRI-SMKNLLNHPwimqdYNYPVEW-----QSKNPFI-H 281
Cdd:cd05600  258 anlyhwkKTLQRPVYTDPDLefnLSDEAWDLITKLI-TDPQDRLqSPEQIKNHP-----FFKNIDWdrlreGSKPPFIpE 331

                 ....
gi 375493532 282 LDDD 285
Cdd:cd05600  332 LESE 335
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
11-259 8.51e-33

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: 126.62  E-value: 8.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK------IMDKNtLGSDLprIKtEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKkvqifeMMDAK-ARQDC--LK-EIDLLQQLNHPNIIKYLASFIENNELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYI---ISQDRLSEEET-RVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGN 160
Cdd:cd08224   78 VLELADAGDLSRLIkhfKKQKRLIPERTiWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL-GRFFSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYD-VPKWLSPSSI 237
Cdd:cd08224  157 KTTAAHSLVGTPYYMSPERIREQGYDFK-SDIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEYPpLPADLYSQEL 235
                        250       260
                 ....*....|....*....|...
gi 375493532 238 L-LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd08224  236 RdLVAACIQPDPEKRPDISYVLD 258
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-263 9.47e-33

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: 126.61  E-value: 9.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPvKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL-KLIDFGLcAKPKGNKDYHLQ 166
Cdd:cd08225   82 DGGDLMKRINRQRGVLFSEDQILswFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGI-ARQLNDSMELAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLLQQMLQ 245
Cdd:cd08225  161 TCVGTPYYLSPEICQNRPY-NNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFaPISPNFSRDLRSLISQLFK 239
                        250
                 ....*....|....*...
gi 375493532 246 VDPKKRISMKNLLNHPWI 263
Cdd:cd08225  240 VSPRDRPSITSILKRPFL 257
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
13-286 2.29e-32

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: 127.35  E-value: 2.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGEMVAIKIMDKNT--LGSDLPRIKTEIEALK-NLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05619    9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVvlMDDDVECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFFVMEYL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCC 169
Cdd:cd05619   89 NGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC-KENMLGDAKTSTFC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPK 249
Cdd:cd05619  168 GTPDYIAPEILLGQKY-NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPE 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 375493532 250 KRISMK-NLLNHPWIMQ-DYNYPVEWQSKNPF---IHLDDDC 286
Cdd:cd05619  247 RRLGVRgDIRQHPFFREiNWEALEEREIEPPFkpkVKSPFDC 288
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
11-263 3.12e-32

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: 125.16  E-value: 3.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFD---YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPKGNKDYH 164
Cdd:cd06610   83 GGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSAslaTGGDRTRKV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELI-QGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKWLSPSSIL-- 238
Cdd:cd06610  163 RKTFVGTPCWMAPEVMeQVRGY-DFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNdppSLETGADYKKYSKSfr 241
                        250       260
                 ....*....|....*....|....*.
gi 375493532 239 -LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06610  242 kMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-271 3.94e-32

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: 125.28  E-value: 3.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRH---QHICQLYHVLETANKIFMVLE 87
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQT 167
Cdd:cd06917   83 YCEGGSIRTLMRAG-PIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKR-ST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELI-QGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKydvPKWL-----SPSSILLLQ 241
Cdd:cd06917  161 FVGTPYWMAPEVItEGKYY-DTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK---PPRLegngySPLLKEFVA 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 242 QMLQVDPKKRISMKNLLNHPWIMQDYNYPV 271
Cdd:cd06917  237 ACLDEEPKDRLSADELLKSKWIKQHSKTPT 266
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
11-252 4.60e-32

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: 125.21  E-value: 4.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNT--LGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNliLRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-------------- 154
Cdd:cd05609   82 VEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmslttnlyeg 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK---W 231
Cdd:cd05609  162 HIEKDTREFLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEgddA 240
                        250       260
                 ....*....|....*....|.
gi 375493532 232 LSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05609  241 LPDDAQDLITRLLQQNPLERL 261
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
17-252 4.98e-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: 126.27  E-value: 4.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD----LPRIKTEIEALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05616    8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDddveCTMVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05616   87 DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMC-KENIWDGVTTKTFCGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05616  166 DYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRL 244
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
11-262 6.18e-32

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: 125.38  E-value: 6.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-----GSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdGINFTALR-EIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPG---GELFDYIIsqdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKD 162
Cdd:cd07841   81 FEFMETdleKVIKDKSI---VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGL-ARSFGSPN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCG--FLPFDDDnvMALYKKIMR-----------GKYDVP 229
Cdd:cd07841  157 RKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRvpFLPGDSD--IDQLGKIFEalgtpteenwpGVTSLP 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 230 KWLSPSS-----------------ILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07841  235 DYVEFKPfpptplkqifpaasddaLDLLQRLLTLNPNKRITARQALEHPY 284
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
57-263 7.18e-32

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: 124.08  E-value: 7.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  57 EIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLK 134
Cdd:cd08221   49 EIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 135 PENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNV 214
Cdd:cd08221  129 TLNIFLTKADLVKLGDFGI-SKVLDSESSMAESIVGTPYYMSPELVQGVKY-NFKSDIWAVGCVLYELLTLKRTFDATNP 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 215 MALYKKIMRGKY-DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd08221  207 LRLAVKIVQGEYeDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
11-262 8.13e-32

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: 125.92  E-value: 8.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05597    3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMlkRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDyIISQ--DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd05597   83 YCGGDLLT-LLSKfeDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQSS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQ----GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM--RGKYDVPKW---LSPSSI 237
Cdd:cd05597  162 VAVGTPDYISPEILQamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPDDeddVSEEAK 241
                        250       260
                 ....*....|....*....|....*...
gi 375493532 238 LLLQQMLQvDPKKRI---SMKNLLNHPW 262
Cdd:cd05597  242 DLIRRLIC-SRERRLgqnGIDDFKKHPF 268
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
11-263 9.00e-32

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: 124.34  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlGSDLPRIKTEIEALKNLRHQH-ICQLYHV------LETANKIF 83
Cdd:cd06608    8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDII--EDEEEEIKLEINILRKFSNHPnIATFYGAfikkdpPGGDDQLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYI----ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKg 159
Cdd:cd06608   86 LVMEYCGGGSVTDLVkglrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLD- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCCGSLAYAAPELIQGKSYL----GSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYkKIMRGKydVPKWLSP 234
Cdd:cd06608  165 STLGRRNTFIGTPYWMAPEVIACDQQPdasyDARCDVWSLGITAIELADGKPPLCDMHPMrALF-KIPRNP--PPTLKSP 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 235 SSIL-----LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06608  242 EKWSkefndFISECLIKNYEQRPFTEELLEHPFI 275
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
11-263 9.70e-32

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: 124.76  E-value: 9.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKS-EEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNkdyhLQ--- 166
Cdd:cd06644   93 GGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKT----LQrrd 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGS----EADVWSMGILLYVLMCGFLPFDDDNVMALYKKImrGKYDVPKWLSPSSILL--- 239
Cdd:cd06644  169 SFIGTPYWMAPEVVMCETMKDTpydyKADIWSLGITLIEMAQIEPPHHELNPMRVLLKI--AKSEPPTLSQPSKWSMefr 246
                        250       260
                 ....*....|....*....|....*.
gi 375493532 240 --LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06644  247 dfLKTALDKHPETRPSAAQLLEHPFV 272
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
10-262 1.07e-31

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: 123.46  E-value: 1.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14107    3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRS--STRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLL--FDEYHKLKLIDFGLCAKPKGNKdyHLQT 167
Cdd:cd14107   81 SSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILmvSPTREDIKICDFGFAQEITPSE--HQFS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK--YDVPKW--LSPSSILLLQQM 243
Cdd:cd14107  159 KYGSPEFVAPEIVH-QEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPEIthLSEDAKDFIKRV 237
                        250
                 ....*....|....*....
gi 375493532 244 LQVDPKKRISMKNLLNHPW 262
Cdd:cd14107  238 LQPDPEKRPSASECLSHEW 256
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
8-252 1.17e-31

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: 126.29  E-value: 1.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLR-HQHICQLYHVLETANKIFM 84
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVhdDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYh 164
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDT- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD---DDNVMA----LYKKIMRGKYDVPKWLSPSSI 237
Cdd:cd05617  173 TSTFCGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFDiitDNPDMNtedyLFQVILEKPIRIPRFLSVKAS 251
                        250
                 ....*....|....*
gi 375493532 238 LLLQQMLQVDPKKRI 252
Cdd:cd05617  252 HVLKGFLNKDPKERL 266
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
11-263 1.72e-31

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: 123.15  E-value: 1.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLgSDLPRIKTEIEALKNLR------HQHICQLYHVLETANKIFM 84
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNNK-DYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCpGGELFDYIiSQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK--LKLIDFG-LCAKPK 158
Cdd:cd14133   79 VFELL-SQNLYEFL-KQNKfqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRcqIKIIDFGsSCFLTQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 gnkdyHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKI--MRGKYDvPKWLSPSS 236
Cdd:cd14133  157 -----RLYSYIQSRYYRAPEVILGLPY-DEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIigTIGIPP-AHMLDQGK 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 237 ------ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14133  230 addelfVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
11-252 2.14e-31

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: 124.72  E-value: 2.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlGSDLPRIKTE--------IEALKNLRHQHICQLYHVLETANKI 82
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKK---GDIIARDEVEslmcekriFETVNSARHPFLVNLFACFQTPEHV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD 162
Cdd:cd05589   78 CFVMEYAAGGDLMMHI-HEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 yHLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQ 242
Cdd:cd05589  157 -RTSTFCGTPEFLAPEVLTDTSYTRA-VDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRR 234
                        250
                 ....*....|
gi 375493532 243 MLQVDPKKRI 252
Cdd:cd05589  235 LLRKNPERRL 244
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
3-260 4.40e-31

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: 122.48  E-value: 4.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   3 DYDELlkyyelhETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHV-LETANk 81
Cdd:cd14046    7 DFEEL-------QVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAwIERAN- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNK 161
Cdd:cd14046   79 LYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQ-----------------TCCGSLAYAAPELIQG-KSYLGSEADVWSMGILLYVlMCgfLPFDDDNVMALYKKIMR 223
Cdd:cd14046  159 ELATQdinkstsaalgssgdltGNVGTALYVAPEVQSGtKSTYNEKVDMYSLGIIFFE-MC--YPFSTGMERVQILTALR 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 375493532 224 GKY-----DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd14046  236 SVSiefppDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
17-265 5.51e-31

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: 123.06  E-value: 5.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIvsRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSLAY 174
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC-KLNMKDDDKTNTFCGTPEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISM 254
Cdd:cd05585  161 LAPELLLGHGYTKA-VDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGY 239
                        250
                 ....*....|....
gi 375493532 255 ---KNLLNHPWIMQ 265
Cdd:cd05585  240 ngaQEIKNHPFFDQ 253
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
9-263 6.67e-31

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: 121.18  E-value: 6.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14110    3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKP--EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-------AKPKGNK 161
Cdd:cd14110   81 CSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAqpfnqgkVLMTDKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQTccgslayAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKW---LSPSSIL 238
Cdd:cd14110  161 GDYVET-------MAPELLEGQG-AGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVN 232
                        250       260
                 ....*....|....*....|....*
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14110  233 FLKSTLCAKPWGRPTASECLQNPWL 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
16-265 7.97e-31

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: 121.30  E-value: 7.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  16 TIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd06605    8 ELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLcakpKGN-KDYHLQTCCGSLA 173
Cdd:cd06605   88 KILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGV----SGQlVDSLAKTFVGTRS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 174 YAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF------DDDNVMALYKKIMRGkyDVPKW----LSPSSILLLQQM 243
Cdd:cd06605  164 YMAPERISGGKY-TVKSDIWSLGLSLVELATGRFPYpppnakPSMMIFELLSYIVDE--PPPLLpsgkFSPDFQDFVSQC 240
                        250       260
                 ....*....|....*....|..
gi 375493532 244 LQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06605  241 LQKDPTERPSYKELMEHPFIKR 262
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
15-265 8.44e-31

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: 121.62  E-value: 8.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIM---DKNtlgsDLPRIKTEIEALKNLR-HQHICQL--YHVLETANKIFMVL-- 86
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEH----DLNVCKREIEIMKRLSgHKNIVGYidSSANRSGNGVYEVLll 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 -EYCPGGELFDYIIS--QDRLSEEETRVVFRQIVSAVAYVHS--QGYAHRDLKPENLLFDEYHKLKLIDFGLCAkpkgNK 161
Cdd:cd14037   85 mEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSAT----TK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQTCCG------------SLAYAAPELI---QGKSyLGSEADVWSMGILLYVLmCGF-LPFDDDNVMAlykkIMRGK 225
Cdd:cd14037  161 ILPPQTKQGvtyveedikkytTLQYRAPEMIdlyRGKP-ITEKSDIWALGCLLYKL-CFYtTPFEESGQLA----ILNGN 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 375493532 226 Y---DVPKWlSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd14037  235 FtfpDNSRY-SKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELA 276
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
33-263 8.64e-31

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: 121.10  E-value: 8.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  33 TGEMVAIKIMDkntLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGgELFDYIISQDRLSEEETRVV 112
Cdd:cd14112   29 TDAHCAVKIFE---VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 113 FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYH--KLKLIDFGLCAK--PKGNKdyhlqTCCGSLAYAAPELIQGKSYLGS 188
Cdd:cd14112  105 VRQILDALHYLHFKGIAHLDVQPDNIMFQSVRswQVKLVDFGRAQKvsKLGKV-----PVDGDTDWASPEFHNPETPITV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 189 EADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYD---VPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14112  180 QSDIWGLGVLTFCLLSGFHPFtsEYDDEEETKENVIFVKCRpnlIFVEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
17-251 1.43e-30

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: 121.40  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHV-----LETANKI-FMVLEY 88
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDknRERWCLEVQIMKKLNHPNVVSARDVppeleKLSPNDLpLLAMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYI---ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENL-LFDEYHKL--KLIDFGLCakpkgnKD 162
Cdd:cd13989   81 CSGGDLRKVLnqpENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRViyKLIDLGYA------KE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCC----GSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF-DDDNVMALYKKI-------------MRG 224
Cdd:cd13989  155 LDQGSLCtsfvGTLQYLAPELFESKKYTCT-VDYWSFGTLAFECITGYRPFlPNWQPVQWHGKVkqkkpehicayedLTG 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 375493532 225 KY----DVPKWLSPSSILL------LQQMLQVDPKKR 251
Cdd:cd13989  234 EVkfssELPSPNHLSSILKeyleswLQLMLRWDPRQR 270
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
9-263 1.84e-30

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: 120.98  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06655   19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDyhl 165
Cdd:cd06655   97 YLAGGSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQitPEQSKR--- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDV--PKWLSPSSILLLQQ 242
Cdd:cd06655  173 STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGTPELqnPEKLSPIFRDFLNR 251
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06655  252 CLEMDVEKRGSAKELLQHPFL 272
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
17-299 2.99e-30

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: 121.91  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKnmVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-------------------A 155
Cdd:cd05610   92 KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdilttpsmA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKgnKDY------------HL-----------------------QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:cd05610  172 KPK--NDYsrtpgqvlslisSLgfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPH-GPAVDWWALGVCLF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 201 VLMCGFLPFDDDNVMALYKKIMrgKYDVPkW------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWImqdynYPVEWQ 274
Cdd:cd05610  249 EFLTGIPPFNDETPQQVFQNIL--NRDIP-WpegeeeLSVNAQNAIEILLTMDPTKRAGLKELKQHPLF-----HGVDWE 320
                        330       340
                 ....*....|....*....|....*....
gi 375493532 275 S----KNPFIHLDDDCVTELSVHHRNNRQ 299
Cdd:cd05610  321 NlqnqTMPFIPQPDDETDTSYFEARNNAQ 349
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
11-285 3.90e-30

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: 121.09  E-value: 3.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMD--KNTLgsDLPRIKTEIEALKNLRHQHICQLYHVL-----ETANKI 82
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNvfDDLI--DAKRILREIKILRHLKHENIIGLLDILrppspEEFNDV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGgELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL-----CAKP 157
Cdd:cd07834   80 YIVTELMET-DLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLargvdPDED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNK-DYhlqtccgsLA---YAAPELIQGKSYLGSEADVWSMGILL--------------YV----LMCGFL--PFDDDN 213
Cdd:cd07834  159 KGFLtEY--------VVtrwYRAPELLLSSKKYTKAIDIWSVGCIFaelltrkplfpgrdYIdqlnLIVEVLgtPSEEDL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 214 VMALYKKIMR-----GKYDVPKW------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHL 282
Cdd:cd07834  231 KFISSEKARNylkslPKKPKKPLsevfpgASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPVAKPPFDFP 310

                 ...
gi 375493532 283 DDD 285
Cdd:cd07834  311 FFD 313
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
11-263 4.07e-30

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: 119.15  E-value: 4.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPkEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQT 167
Cdd:cd08218   82 DGGDLYKRINAQRGVLFPEDQILdwFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGI-ARVLNSTVELART 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLLQQMLQV 246
Cdd:cd08218  161 CIGTPYYLSPEICENKPY-NNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKR 239
                        250
                 ....*....|....*..
gi 375493532 247 DPKKRISMKNLLNHPWI 263
Cdd:cd08218  240 NPRDRPSINSILEKPFI 256
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
17-252 5.43e-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: 120.87  E-value: 5.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD----LPRIKTEIEALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05615   18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDddveCTMVEKRVLALQD-KPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05615   97 DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC-KEHMVEGVTTRTFCGTP 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05615  176 DYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRL 254
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
11-263 5.67e-30

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: 118.97  E-value: 5.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIM----DKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLE--TANKIFM 84
Cdd:cd06653    4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnkdyh 164
Cdd:cd06653   84 FVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR-------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCC----------GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR--GKYDVPKWL 232
Cdd:cd06653  156 IQTICmsgtgiksvtGTPYWMSPEVISGEGY-GRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATqpTKPQLPDGV 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 375493532 233 SPSSILLLQQMLqVDPKKRISMKNLLNHPWI 263
Cdd:cd06653  235 SDACRDFLRQIF-VEEKRRPTAEFLLRHPFV 264
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
17-252 5.88e-30

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 120.19  E-value: 5.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIE----ALKNlRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEkrvlALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLQTCCGSL 172
Cdd:cd05587   83 DLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC-KEGIFGGKTTRTFCGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05587  162 DYIAPEIIAYQPY-GKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
8-272 6.09e-30

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: 119.78  E-value: 6.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKI--MDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVL--ETANKIF 83
Cdd:cd07845    6 VTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKvrMDNERDGIPISSLR-EITLLLNLRHPNIVELKEVVvgKHLDSIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPG--GELFDYIisQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNK 161
Cdd:cd07845   85 LVMEYCEQdlASLLDNM--PTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGL-ARTYGLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVL------------------MCGFLPFDDDNVMALYKKI-M 222
Cdd:cd07845  162 AKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELlahkpllpgkseieqldlIIQLLGTPNESIWPGFSDLpL 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493532 223 RGKYDVPK-----------WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWiMQDYNYPVE 272
Cdd:cd07845  242 VGKFTLPKqpynnlkhkfpWLSEAGLRLLNFLLMYDPKKRATAEEALESSY-FKEKPLPCE 301
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
15-260 7.69e-30

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: 118.41  E-value: 7.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAchILTGE-----MVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd00192    1 KKLGEGAFGEVYKG--KLKGGdgktvDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVF---------RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGN 160
Cdd:cd00192   79 EGGDLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL-SRDIYD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSL--AYAAPELIQGKSYlgSEA-DVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPS 235
Cdd:cd00192  158 DDYYRKKTGGKLpiRWMAPESLKDGIF--TSKsDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKGYRlPKPENCPDE 235
                        250       260
                 ....*....|....*....|....*
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd00192  236 LYELMLSCWQLDPEDRPTFSELVER 260
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-222 7.97e-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: 7.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   2 KDYDELLKYYELH-------ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgsdLPRIKT-----EIEALKNLRHQHI 69
Cdd:cd05624   58 KPFTQLVKEMQLHrddfeiiKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEM---LKRAETacfreERNVLVNGDCQWI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  70 CQLYHVLETANKIFMVLEYCPGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKL 148
Cdd:cd05624  135 TTLHYAFQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLCAKPkgNKDYHLQT--CCGSLAYAAPELIQ----GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM 222
Cdd:cd05624  215 ADFGSCLKM--NDDGTVQSsvAVGTPDYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-263 1.25e-29

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: 118.10  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYEL-HETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDL-PRIKTEI---EALKNlrHQHICQLYHVLETA 79
Cdd:cd14198    3 DNFNNFYILtSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCrAEILHEIavlELAKS--NPRVVNLHEVYETT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELFDYIISQ--DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL---KLIDFGLc 154
Cdd:cd14198   81 SEIILILEYAAGGEIFNLCVPDlaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgdiKIVDFGM- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDyHLQTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK---- 230
Cdd:cd14198  160 SRKIGHAC-ELREIMGTPEYLAPEILNYDP-ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfs 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 231 WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14198  238 SVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-251 2.54e-29

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: 117.22  E-value: 2.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLAC-HILTGEMVAIK-------IMDKNTLGSD--LPRIKTEIEALK-NLRHQHICQLYHVLETA 79
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRkKSNGQTLLALKeinmtnpAFGRTEQERDksVGDIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELFDYIIS----QDRLSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLc 154
Cdd:cd08528   82 DRLYIVMELIEGAPLGEHFSSlkekNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFGL- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVlMCGFLP-FDDDNVMALYKKIMRGKYD-VPKWL 232
Cdd:cd08528  161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPY-GEKADIWALGCILYQ-MCTLQPpFYSTNMLTLATKIVEAEYEpLPEGM 238
                        250       260
                 ....*....|....*....|
gi 375493532 233 -SPSSILLLQQMLQVDPKKR 251
Cdd:cd08528  239 ySDDITFVIRSCLTPDPEAR 258
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
11-260 2.89e-29

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: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKimdKNTLGS--DLPRIKTEIEALKNLRHQHICQL--YHVLETAN---KIF 83
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALK---KILCHSkeDVKEAMREIENYRLFNHPNILRLldSQIVKEAGgkkEVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYI----ISQDRLSEEETRVVFRQIVSAVAYVHSQ---GYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd13986   79 LLLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMNP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 P----KGN------KDYHLQTCcgSLAYAAPELIQGKSY--LGSEADVWSMGILLYVLMCGFLPFD------DDNVMAly 218
Cdd:cd13986  159 ArieiEGRrealalQDWAAEHC--TMPYRAPELFDVKSHctIDEKTDIWSLGCTLYALMYGESPFErifqkgDSLALA-- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 219 kkIMRGKYdvpKWLSPSSIL-----LLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd13986  235 --VLSGNY---SFPDNSRYSeelhqLVKSMLVVNPAERPSIDDLLSR 276
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
17-262 3.82e-29

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: 118.29  E-value: 3.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKN--TLGSDLPRIKTE---IEALKNlrHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIKKElvNDDEDIDWVQTEkhvFETASN--HPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYhLQTCCGS 171
Cdd:cd05588   81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT-TSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD--------DDNVMA-LYKKIMRGKYDVPKWLSPSSILLLQQ 242
Cdd:cd05588  160 PNYIAPEILRGEDY-GFSVDWWALGVLMFEMLAGRSPFDivgssdnpDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKG 238
                        250       260
                 ....*....|....*....|....*.
gi 375493532 243 MLQVDPKKRI------SMKNLLNHPW 262
Cdd:cd05588  239 FLNKNPAERLgchpqtGFADIQSHPF 264
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
16-280 4.30e-29

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 118.19  E-value: 4.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  16 TIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgsdLPR-----IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05598    8 TIGVGAFGEVSLVRKKDTNALYAMKTLRKKDV---LKRnqvahVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDYIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA--KPKGNKDYHL-QT 167
Cdd:cd05598   85 GGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfRWTHDSKYYLaHS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM--RGKYDVPKW--LSPSSILLLQQM 243
Cdd:cd05598  165 LVGTPNYIAPEVLLRTGYTQL-CDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLSPEAKDLILRL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 375493532 244 LqVDPKKRISMKN---LLNHPWiMQDYNYPVEWQSKNPFI 280
Cdd:cd05598  244 C-CDAEDRLGRNGadeIKAHPF-FAGIDWEKLRKQKAPYI 281
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
11-225 4.99e-29

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: 119.73  E-value: 4.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgsdLPRIKT-----EIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEM---LKRAETacfreERDVLVNGDSQWITTLHYAFQDDNNLYLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYH 164
Cdd:cd05623  151 MDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQ 230
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 165 LQTCCGSLAYAAPELIQ----GKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd05623  231 SSVAVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHK 295
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
9-261 7.58e-29

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: 115.40  E-value: 7.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILT-------GEMVAIKIMDKNTLGSdlpRIKTEIEALKNLRHQH-ICQLYHVLETAN 80
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPS---RILNELECLERLGGSNnVSGLITAFRNED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIisqDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGL----CA 155
Cdd:cd14019   78 QVVAVLPYIEHDDFRDFY---RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLaqreED 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KP--KGNkdyhlqtCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPF--DDDNVMALyKKIM--RGKYDVp 229
Cdd:cd14019  155 RPeqRAP-------RAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPFffSSDDIDAL-AEIAtiFGSDEA- 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 230 kwlspssILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14019  226 -------YDLLDKLLELDPSKRITAEEALKHP 250
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
15-262 1.97e-28

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: 114.89  E-value: 1.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNT-LGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGgE 93
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLDAeEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEYMDK-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYI-ISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCCG 170
Cdd:cd07836   84 LKKYMdTHGVRgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGL-ARAFGIPVNTFSNEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-----------GKYDVPKW-------- 231
Cdd:cd07836  163 TLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtptestwpGISQLPEYkptfpryp 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 375493532 232 ----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07836  243 pqdlqqlfphADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
11-263 1.97e-28

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: 114.37  E-value: 1.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIM----DKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVL----ETANKI 82
Cdd:cd06652    4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfdpESPETSKEVNALECEIQLLKNLLHERIVQYYGCLrdpqERTLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMvlEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnkd 162
Cdd:cd06652   84 FM--EYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKR------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 yhLQTCC----------GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD--VPK 230
Cdd:cd06652  156 --LQTIClsgtgmksvtGTPYWMSPEVISGEGY-GRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNpqLPA 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 231 WLSPSSILLLQQMLqVDPKKRISMKNLLNHPWI 263
Cdd:cd06652  233 HVSDHCRDFLKRIF-VEAKLRPSADELLRHTFV 264
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
10-271 2.67e-28

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: 114.74  E-value: 2.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd06643    6 FWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKS-EEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTC 168
Cdd:cd06643   85 AGGAVDAVMLELERpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRR-DSF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELI-----QGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKImrGKYDVPKWLSPSSIL----- 238
Cdd:cd06643  164 IGTPYWMAPEVVmcetsKDRPY-DYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKI--AKSEPPTLAQPSRWSpefkd 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWI-MQDYNYPV 271
Cdd:cd06643  241 FLRKCLEKNVDARWTTSQLLQHPFVsVLVSNKPL 274
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
66-263 3.63e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 113.80  E-value: 3.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  66 HQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY-H 144
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkD 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 145 KLKLIDFGLCaKPKGnkdyhlQTCC--GSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDN-------VM 215
Cdd:PHA03390 148 RIYLCDYGLC-KIIG------TPSCydGTLDYFSPEKIKGHNYDVS-FDWWAVGVLTYELLTGKHPFKEDEdeeldleSL 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 216 A--LYKKIMRgkydvPKWLSPSSILLLQQMLQVDPKKR-ISMKNLLNHPWI 263
Cdd:PHA03390 220 LkrQQKKLPF-----IKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFL 265
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
9-261 4.55e-28

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 118.05  E-value: 4.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNlrhqhiCQLYHVL----------- 76
Cdd:PTZ00283  32 KKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSeADKNRAQAEVCCLLN------CDFFSIVkchedfakkdp 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  77 ---ETANKIFMVLEYCPGGELFDYIISQDRLS----EEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLI 149
Cdd:PTZ00283 106 rnpENVLMIALVLDYANAGDLRQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLG 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 150 DFGLcAKPKGN--KDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD 227
Cdd:PTZ00283 186 DFGF-SKMYAAtvSDDVGRTFCGTPYYVAPEIWRRKPY-SKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYD 263
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 228 -VPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:PTZ00283 264 pLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
9-263 4.61e-28

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: 114.43  E-value: 4.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06656   19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNlQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDyhl 165
Cdd:cd06656   97 YLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitPEQSKR--- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDV--PKWLSPSSILLLQQ 242
Cdd:cd06656  173 STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGTPELqnPERLSAVFRDFLNR 251
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06656  252 CLEMDVDRRGSAKELLQHPFL 272
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
11-263 5.07e-28

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: 113.86  E-value: 5.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK--IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVL--ETANKIFMVL 86
Cdd:cd07843    7 YEKLNRIEEGTYGVVYRARDKKTGEIVALKklKMEKEKEGFPITSLR-EINILLKLQHPNIVTVKEVVvgSNLDKIYMVM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGgELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHL 165
Cdd:cd07843   86 EYVEH-DLKSLMeTMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL-AREYGSPLKPY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-----------GKYDVPKW--- 231
Cdd:cd07843  164 TQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKllgtptekiwpGFSELPGAkkk 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 232 ------------------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07843  244 tftkypynqlrkkfpalsLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
17-222 7.17e-28

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: 115.72  E-value: 7.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05629    9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMfkKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-------------------- 154
Cdd:cd05629   89 MTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayyqkllqgks 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKP--------------------------KGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLP 208
Cdd:cd05629  169 NKNridnrnsvavdsinltmsskdqiatwKKNRRLMAYSTVGTPDYIAPEIFLQQGY-GQECDWWSLGAIMFECLIGWPP 247
                        250
                 ....*....|....
gi 375493532 209 FDDDNVMALYKKIM 222
Cdd:cd05629  248 FCSENSHETYRKII 261
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
17-252 8.29e-28

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: 114.20  E-value: 8.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSdlpriKTEIEALKNLRHQHICQ----------LYHVLETANKIFMVL 86
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVA-----KKEVAHTIGERNILVRTaldespfivgLKFSFQTPTDLYLVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:cd05586   76 DYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL-SKADLTDNKTTN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK-WLSPSSILLLQQMLQ 245
Cdd:cd05586  155 TFCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLN 234

                 ....*..
gi 375493532 246 VDPKKRI 252
Cdd:cd05586  235 RNPKHRL 241
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
11-261 8.46e-28

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: 113.79  E-value: 8.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTlgsDLPRIKTEIEALKNLR-HQHICQLYHVLETANK--IFMVLE 87
Cdd:cd14132   20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL-KPV---KKKKIKREIKILQNLRgGPNIVKLLDVVKDPQSktPSLIFE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGgELFDYIISQdrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKGNKDYhlQ 166
Cdd:cd14132   96 YVNN-TDFKTLYPT--LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLAEFYHPGQEY--N 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILL-------YVLMCGF----------------------------LPFDD 211
Cdd:cd14132  171 VRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLasmifrkEPFFHGHdnydqlvkiakvlgtddlyayldkygieLPPRL 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 212 DNVMALYKKIMRGKY---DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14132  251 NDILGRHSKKPWERFvnsENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
11-258 1.01e-27

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: 112.37  E-value: 1.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQD-RLSEEETRVV-FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKPKGNKDYHLQTC 168
Cdd:cd08219   82 GGDLMQKIKLQRgKLFPEDTILQwFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLTSPGAYACTY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD-VPKWLSPSSILLLQQMLQVD 247
Cdd:cd08219  161 VGTPYYVPPEIWENMPY-NNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKRN 239
                        250
                 ....*....|.
gi 375493532 248 PKKRISMKNLL 258
Cdd:cd08219  240 PRSRPSATTIL 250
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
17-270 1.91e-27

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: 111.85  E-value: 1.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVkLACHIL-TGEMVAIKIMDKNTL----GSDLPRIKTEIEALKNLRHqhICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05577    1 LGRGGFGEV-CACQVKaTGKMYACKKLDKKRIkkkkGETMALNEKIILEKVSSPF--IVSLAYAFETKDKLCLVLTLMNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTcc 169
Cdd:cd05577   78 GDLKYHIYNVGTRGFSEARAIFyaAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRV-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV----PKWLSPSSILLLQQMLQ 245
Cdd:cd05577  156 GTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMaveyPDSFSPEARSLCEGLLQ 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 246 VDPKKRI-----SMKNLLNHPwIMQDYNYP 270
Cdd:cd05577  236 KDPERRLgcrggSADEVKEHP-FFRSLNWQ 264
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
17-261 2.13e-27

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: 111.75  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMD--KNTLGSD---LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY-HKLKLIDFG----LCAKPKGNKDYHLQ 166
Cdd:cd06630   88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGaaarLASKGTGAGEFQGQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TcCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNV---MALYKKIM--RGKYDVPKWLSPSSILLLQ 241
Cdd:cd06630  168 L-LGTIAFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAEKIsnhLALIFKIAsaTTPPPIPEHLSPGLRDVTL 245
                        250       260
                 ....*....|....*....|
gi 375493532 242 QMLQVDPKKRISMKNLLNHP 261
Cdd:cd06630  246 RCLELQPEDRPPARELLKHP 265
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
8-262 2.27e-27

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 113.15  E-value: 2.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELH--ETIGTGGFAKVKLACHiLTGEM--VAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANK 81
Cdd:PTZ00426  27 MKYEDFNfiRTLGTGSFGRVILATY-KNEDFppVAIKRFEKSKIikQKQVDHVFSERKILNYINHPFCVNLYGSFKDESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNK 161
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGF-AKVVDTR 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYhlqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQ 241
Cdd:PTZ00426 185 TY---TLCGTPEYIAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMK 260
                        250       260
                 ....*....|....*....|....*.
gi 375493532 242 QMLQVDPKKRI-----SMKNLLNHPW 262
Cdd:PTZ00426 261 KLLSHDLTKRYgnlkkGAQNVKEHPW 286
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
11-265 5.04e-27

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: 110.72  E-value: 5.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdkNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFV--KVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY--HKLKLIDFGLCAKPKGNKDYHLQT 167
Cdd:cd14104   80 GVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQLKPGDKFRLQY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CcgSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY----DVPKWLSPSSILLLQQM 243
Cdd:cd14104  160 T--SAEFYAPEVHQHES-VSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYafddEAFKNISIEALDFVDRL 236
                        250       260
                 ....*....|....*....|..
gi 375493532 244 LQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd14104  237 LVKERKSRMTAQEALNHPWLKQ 258
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
17-263 6.83e-27

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: 110.88  E-value: 6.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDlRKQQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPkgNKDY-HLQTCCGSLAY 174
Cdd:cd06657  106 D-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV--SKEVpRRKSLVGTPYW 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDD---NVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd06657  183 MAPELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEpplKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
                        250
                 ....*....|..
gi 375493532 252 ISMKNLLNHPWI 263
Cdd:cd06657  262 ATAAELLKHPFL 273
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
11-263 7.21e-27

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: 109.82  E-value: 7.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR--IKTEIEA--LKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDetVDANREAklLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELfDYIISQDRLSEE---ETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLlFDEYHKLKLIDFGLCAKPKGNK 161
Cdd:cd08222   82 EYCEGGDL-DDKISEYKKSGTtidENQILdwFIQLLLAVQYMHERRILHRDLKAKNI-FLKNNVIKVGDFGISRILMGTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYhLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLL 240
Cdd:cd08222  160 DL-ATTFTGTPYYMSPEVLKHEGY-NSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIY 237
                        250       260
                 ....*....|....*....|...
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd08222  238 SRMLNKDPALRPSAAEILKIPFI 260
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
97-260 8.28e-27

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: 110.57  E-value: 8.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY-HKLKLIDFGLcAKPKGNKDYHLQTCCGSLAYA 175
Cdd:cd13974  122 YVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRtRKITITNFCL-GKHLVSEDDLLKDQRGSPAYI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 176 APELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK--WLSPSSILLLQQMLQVDPKKRIS 253
Cdd:cd13974  201 SPDVLSGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRLT 280

                 ....*..
gi 375493532 254 MKNLLNH 260
Cdd:cd13974  281 ASEVLDS 287
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
15-260 8.75e-27

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: 109.89  E-value: 8.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgsdlPRIKTEIEALKNLRHQHICQLY-------HVLETANK------ 81
Cdd:cd14047   12 ELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNN-----EKAEREVKALAKLDHPNIVRYNgcwdgfdYDPETSSSnssrsk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 ---IFMVLEYCPGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd14047   87 tkcLFIQMEFCEKGTLESWIekRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGnkDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLmcgFLPFDDDNVMALYKKIMRGKyDVPKWLS--- 233
Cdd:cd14047  167 LKN--DGKRTKSKGTLSYMSPEQISSQDY-GKEVDIYALGLILFEL---LHVCDSAFEKSKFWTDLRNG-ILPDIFDkry 239
                        250       260
                 ....*....|....*....|....*..
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd14047  240 KIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
17-262 8.96e-27

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: 109.79  E-value: 8.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM----DKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVL----ETANKIFMvlEY 88
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVqfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLrdraEKTLTIFM--EY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnkdyhLQTC 168
Cdd:cd06651   93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR--------LQTI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 C----------GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD--VPKWLSPSS 236
Cdd:cd06651  165 CmsgtgirsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNpqLPSHISEHA 243
                        250       260
                 ....*....|....*....|....*.
gi 375493532 237 ILLLQQMLqVDPKKRISMKNLLNHPW 262
Cdd:cd06651  244 RDFLGCIF-VEARHRPSAEELLRHPF 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
11-262 9.21e-27

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: 110.06  E-value: 9.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPrIKT--EIEALKNLR---HQHICQLY---HVLETAN-- 80
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIP-LSTirEIALLKQLEsfeHPNVVRLLdvcHGPRTDRel 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGgELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPK 158
Cdd:cd07838   80 KLTLVFEHVDQ-DLATYLdkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGL-ARIY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNkDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLY------VLMCGF--------------LPFDDD---NVM 215
Cdd:cd07838  158 SF-EMALTSVVVTLWYRAPEVLLQSSY-ATPVDMWSVGCIFAelfnrrPLFRGSseadqlgkifdvigLPSEEEwprNSA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 216 AL-----YKKIMRGKYDVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07838  236 LPrssfpSYTPRPFKSFVPE-IDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
9-263 1.05e-26

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: 110.20  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06654   20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNlQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGNKDyhl 165
Cdd:cd06654   98 YLAGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitPEQSKR--- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDV--PKWLSPSSILLLQQ 242
Cdd:cd06654  174 STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGTPELqnPEKLSAIFRDFLNR 252
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06654  253 CLEMDVEKRGSAKELLQHQFL 273
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-263 1.23e-26

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: 109.06  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlGSDLPRIKTEIEA--LKNLRHQHICQLYHVLETANK-IFMVLE 87
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKN-ASKRERKAAEQEAklLSKLKHPNIVSYKESFEGEDGfLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYhL 165
Cdd:cd08223   81 FCEGGDLYTRLKEQKGVLLEERQVVewFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDM-A 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPSSILLLQQML 244
Cdd:cd08223  160 TTLIGTPYYMSPELFSNKPY-NHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAML 238
                        250
                 ....*....|....*....
gi 375493532 245 QVDPKKRISMKNLLNHPWI 263
Cdd:cd08223  239 HQDPEKRPSVKRILRQPYI 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
11-219 1.27e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 114.12  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLA-CHILtGEMVAIKIMdKNTLGSD---LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAkDTRL-DRDVAVKVL-RPDLARDpefVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHlQ 166
Cdd:NF033483  87 EYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI-ARALSSTTMT-Q 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 167 T--CCGSLAYAAPELIQGkSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMA-LYK 219
Cdd:NF033483 165 TnsVLGTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFDGDSPVSvAYK 219
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
8-225 1.30e-26

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 111.69  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMleKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGN----- 160
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAhrtef 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 ---------KDYHLQ--------------------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDD 211
Cdd:cd05627  161 yrnlthnppSDFSFQnmnskrkaetwkknrrqlaySTVGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCS 239
                        250
                 ....*....|....
gi 375493532 212 DNVMALYKKIMRGK 225
Cdd:cd05627  240 ETPQETYRKVMNWK 253
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
15-263 1.40e-26

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: 109.06  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVklACHIL-TGEMVAIK-----IMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd06631    7 NVLGKGAYGTV--YCGLTsTGQLIAVKqveldTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAK------PKGNKD 162
Cdd:cd06631   85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG-CAKrlcinlSSGSQS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKW---LSPSSILL 239
Cdd:cd06631  164 QLLKSMRGTPYWMAPEVINETGH-GRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLpdkFSPEARDF 242
                        250       260
                 ....*....|....*....|....
gi 375493532 240 LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06631  243 VHACLTRDQDERPSAEQLLKHPFI 266
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
11-212 1.65e-26

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: 109.33  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR---IK---TEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKqnyIKhalREYEIHKSLDHPRIVKLYDVFEIDTDSFC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 -VLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYV--HSQGYAHRDLKPENLLFDEYHK---LKLIDFGLCaKPK 158
Cdd:cd13990   82 tVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVsgeIKITDFGLS-KIM 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493532 159 GNKDYHLQTC------CGSLAYAAPE-LIQGKSY--LGSEADVWSMGILLYVLMCGFLPFDDD 212
Cdd:cd13990  161 DDESYNSDGMeltsqgAGTYWYLPPEcFVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFGHN 223
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
17-263 2.54e-26

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: 108.97  E-value: 2.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDlRKQQRREL--LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-----PKgnkdyhLQTCCG 170
Cdd:cd06658  108 D-IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQvskevPK------RKSLVG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKImrgKYDVPKWLSP----SSIL--LLQQML 244
Cdd:cd06658  181 TPYWMAPEVISRLPY-GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRI---RDNLPPRVKDshkvSSVLrgFLDLML 256
                        250
                 ....*....|....*....
gi 375493532 245 QVDPKKRISMKNLLNHPWI 263
Cdd:cd06658  257 VREPSQRATAQELLQHPFL 275
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
11-263 2.73e-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: 109.56  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLpRIKTEIEALKNLRHQHICQLYHVLE-TANKIF-----M 84
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-RNKKRFHQ-QALVEVKILKHLNDNDPDDKHNIVRyKDSFIFrghlcI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCpGGELFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK--LKLIDFGlCAKPKGN 160
Cdd:cd14210   93 VFELL-SINLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFG-SSCFEGE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDY-HLQtccgSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM----------------- 222
Cdd:cd14210  171 KVYtYIQ----SRFYRAPEVILGLPY-DTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMevlgvppkslidkasrr 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 223 ----------------RGKYDVP---------KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14210  246 kkffdsngkprpttnsKGKKRRPgskslaqvlKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
6-293 4.87e-26

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 109.31  E-value: 4.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   6 ELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgsdlP--------RIKTEIEALKNLRHQHICQLYHV-- 75
Cdd:cd07851   12 EVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSR-------PfqsaihakRTYRELRLLKHMKHENVIGLLDVft 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  76 ----LETANKIFMVLEYCpGGELFDYIISQdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDF 151
Cdd:cd07851   85 passLEDFQDVYLVTHLM-GADLNNIVKCQ-KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 152 GLcAKPkgnKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM--------- 222
Cdd:cd07851  163 GL-ARH---TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMnlvgtpdee 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 --------------RGKYDVPK--------WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWiMQDYNYPVEWQSKNPFI 280
Cdd:cd07851  239 llkkissesarnyiQSLPQMPKkdfkevfsGANPLAIDLLEKMLVLDPDKRITAAEALAHPY-LAEYHDPEDEPVAPPYD 317
                        330
                 ....*....|...
gi 375493532 281 HLDDDcvTELSVH 293
Cdd:cd07851  318 QSFES--RDLTVD 328
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
11-263 1.04e-25

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: 106.72  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHET-----IGTGGFAKVKLACHILTGEMVAIK-IMDKNTlgSDLPRIKTEIEALKNLRHQHICQLYHVLETAN--KI 82
Cdd:cd06624    5 YEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKeIPERDS--REVQPLHEEIALHSRLSHKNIVQYLGSVSEDGffKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMvlEYCPGGELFDYIISQ-DRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK-LKLIDFGLCAKPK 158
Cdd:cd06624   83 FM--EQVPGGSLSALLRSKwGPLKDNENTIGYytKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGvVKISDFGTSKRLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GnkdyhLQTCC----GSLAYAAPELI-QGKSYLGSEADVWSMGILLYVLMCGFLPFDD--DNVMALYKKIMRGKY-DVPK 230
Cdd:cd06624  161 G-----INPCTetftGTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMFKVGMFKIHpEIPE 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 231 WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06624  236 SLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
11-262 1.07e-25

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: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVL-----ETANKIFM 84
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKkINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCpGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNK--- 161
Cdd:cd07859   82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGL-ARVAFNDtpt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 -----DYhlqtcCGSLAYAAPELIqgKSYLG---SEADVWSMGILLYVLMCGFLPFDDDNVM------------------ 215
Cdd:cd07859  160 aifwtDY-----VATRWYRAPELC--GSFFSkytPAIDIWSIGCIFAEVLTGKPLFPGKNVVhqldlitdllgtpspeti 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 216 --------ALYKKIMRGKYDVP---KW--LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07859  233 srvrnekaRRYLSSMRKKQPVPfsqKFpnADPLALRLLERLLAFDPKDRPTAEEALADPY 292
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
11-225 1.10e-25

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: 108.97  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05628    3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMleKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGN-------- 160
Cdd:cd05628   83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAhrtefyrn 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 ------KDYHLQ--------------------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNV 214
Cdd:cd05628  163 lnhslpSDFTFQnmnskrkaetwkrnrrqlafSTVGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCSETP 241
                        250
                 ....*....|.
gi 375493532 215 MALYKKIMRGK 225
Cdd:cd05628  242 QETYKKVMNWK 252
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
52-263 1.38e-25

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: 106.06  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  52 PRIKTEIEALKNLRHQHICQLYHVLETANK-IFMVLEYCPGGELF--DYIISQDRLSEEETRVVFRQIVSAVAYVHSQGY 128
Cdd:cd14109   41 PFLMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 129 AHRDLKPENLLFdEYHKLKLIDFGLCAKPKGNKDYHLQTccGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLP 208
Cdd:cd14109  121 AHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTTLIY--GSPEFVSPEIVNSYP-VTLATDMWSVGVLTYVLLGGISP 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 209 FDDDNVMALYKKIMRGKY--DVPKW--LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd14109  197 FLGDNDRETLTNVRSGKWsfDSSPLgnISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
11-262 3.00e-25

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: 105.82  E-value: 3.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLR-HQHICQLYHVL--ETANKIFMVLE 87
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNILRLIEVLfdRKTGRLALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGgELFDYIisQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHkLKLIDFGLCAKPKGNKDY- 163
Cdd:cd07831   81 LMDM-NLYELI--KGRkrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI-LKLADFGSCRGIYSKPPYt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 -HLQTccgsLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDN------------------VMALYKKIMRG 224
Cdd:cd07831  157 eYIST----RWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNeldqiakihdvlgtpdaeVLKKFRKSRHM 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 225 KYDVPK-------WL----SPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07831  233 NYNFPSkkgtglrKLlpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
11-263 3.87e-25

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: 105.11  E-value: 3.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII-KLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCCG 170
Cdd:cd06646   90 GGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKR-KSFIG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPEL--IQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP------KWlSPSSILLLQQ 242
Cdd:cd06646  169 TPYWMAPEVaaVEKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPklkdktKW-SSTFHNFVKI 247
                        250       260
                 ....*....|....*....|.
gi 375493532 243 MLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06646  248 SLTKNPKKRPTAERLLTHLFV 268
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
11-262 3.98e-25

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: 105.58  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKT-EIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG----LCAKPKGNKDYhl 165
Cdd:cd07846   83 DHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGfartLAAPGEVYTDY-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 qtcCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCG--FLPFDDDnVMALYKKI---------------------- 221
Cdd:cd07846  161 ---VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGepLFPGDSD-IDQLYHIIkclgnliprhqelfqknplfag 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 222 -----------MRGKYdvPKWlSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07846  237 vrlpevkevepLERRY--PKL-SGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
MARK_C_like cd12121
C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
514-608 4.52e-25

C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases, and similar domains; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. In yeast, MARK/Par-1 homologs are called Kin1/2 kinases. Kin1 is a membrane-associated kinase that is involved in regulating cytokinesis and the cell surface. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213377  Cd Length: 96  Bit Score: 99.22  E-value: 4.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 514 RRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKG-YTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKG 592
Cdd:cd12121    1 RSLRGPFSVATTSTKSPEEIMNEIKRVLRSNGIDYEEVGgYLLECKHGDSSGGEFVIFEIEICKLPRLGLNGIRFKRISG 80
                         90
                 ....*....|....*.
gi 375493532 593 DAWVYKRLVEDILSSC 608
Cdd:cd12121   81 DSWQYKRLCKKILNEL 96
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
11-265 5.33e-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: 104.74  E-value: 5.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd06645   13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVI-KLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlQTCCG 170
Cdd:cd06645   92 GGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR-KSFIG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 171 SLAYAAPEL--IQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVP------KWlSPSSILLLQQ 242
Cdd:cd06645  171 TPYWMAPEVaaVERKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPklkdkmKW-SNSFHHFVKM 249
                        250       260
                 ....*....|....*....|...
gi 375493532 243 MLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06645  250 ALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
17-267 7.10e-25

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: 104.06  E-value: 7.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDKNTLGSDlprIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14058    1 VGRGSFGVVCKA--RWRNQIVAVKIIESESEKKA---FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFR---QIVSAVAYVHS---QGYAHRDLKPENLLFDEYHK-LKLIDFGLCAkpkgNKDYHLQTCC 169
Cdd:cd14058   76 VLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTvLKICDFGTAC----DISTHMTNNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlgSE-ADVWSMGILLYVLMCGFLPFDD-DNVMALY-KKIMRGKY-----DVPKWLSPssilLLQ 241
Cdd:cd14058  152 GSAAWMAPEVFEGSKY--SEkCDVFSWGIILWEVITRRKPFDHiGGPAFRImWAVHNGERpplikNCPKPIES----LMT 225
                        250       260
                 ....*....|....*....|....*....
gi 375493532 242 QMLQVDPKKRISMKNL---LNHpwIMQDY 267
Cdd:cd14058  226 RCWSKDPEKRPSMKEIvkiMSH--LMQFF 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
17-265 8.25e-25

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 106.06  E-value: 8.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDR-LSEeetrvVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyHLQTCCGSLAYA 175
Cdd:PLN00034 162 THIADEQfLAD-----VARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMD-PCNSSVGTIAYM 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 176 APELI-----QGKsYLGSEADVWSMGILLYVLMCGFLPF---DDDNVMALYKKI-MRGKYDVPKWLSPSSILLLQQMLQV 246
Cdd:PLN00034 236 SPERIntdlnHGA-YDGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAIcMSQPPEAPATASREFRHFISCCLQR 314
                        250
                 ....*....|....*....
gi 375493532 247 DPKKRISMKNLLNHPWIMQ 265
Cdd:PLN00034 315 EPAKRWSAMQLLQHPFILR 333
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
5-202 1.18e-24

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: 104.00  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELhetIGTGGFAKVKLACHIL----TGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA- 79
Cdd:cd05038    3 ERHLKFIKQ---LGEGHFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 -NKIFMVLEYCPGGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKP 157
Cdd:cd05038   80 rRSLRLIMEYLPSGSLRDYLqRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 158 KGNKDYHLQTCCGSLA--YAAPELIQgKSYLGSEADVWSMGILLYVL 202
Cdd:cd05038  160 PEDKEYYYVKEPGESPifWYAPECLR-ESRFSSASDVWSFGVTLYEL 205
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
12-258 1.42e-24

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: 103.58  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLA-CHiltGEmVAIKIMDKNTLGSD-LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14063    3 EIKEVIGKGRFGRVHRGrWH---GD-VAIKLLNIDYLNEEqLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQ-DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEyHKLKLIDFGLCA----KPKGNKDYH 164
Cdd:cd14063   79 KGRTLYSLIHERkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlsglLQPGRREDT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCCGSLAYAAPELI---------QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK------YDVP 229
Cdd:cd14063  158 LVIPNGWLCYLAPEIIralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKkqslsqLDIG 237
                        250       260
                 ....*....|....*....|....*....
gi 375493532 230 KWLSPssilLLQQMLQVDPKKRISMKNLL 258
Cdd:cd14063  238 REVKD----ILMQCWAYDPEKRPTFSDLL 262
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
11-261 1.75e-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: 103.27  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKV-KLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLR---HQHICQLYHVLETANKIFMV 85
Cdd:cd14052    2 FANVELIGSGEFSQVyKVSERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDRLSE-EETRV--VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD 162
Cdd:cd14052   82 TELCENGSLDVFLSELGLLGRlDEFRVwkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLIRG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQtccGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGF-LPfddDNVMAlYKKIMRGKY-DVP--KWLSPSSIL 238
Cdd:cd14052  162 IERE---GDREYIAPEILSEHMY-DKPADIFSLGLILLEAAANVvLP---DNGDA-WQKLRSGDLsDAPrlSSTDLHSAS 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 375493532 239 ----------------------LLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14052  234 spssnpppdppnmpilsgsldrVVRWMLSPEPDRRPTADDVLATP 278
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
17-209 1.94e-24

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: 103.50  E-value: 1.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKI------FMVLEYCP 90
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYCQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKL---KLIDFGLCakpkgnKDYH 164
Cdd:cd14038   82 GGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYA------KELD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 165 LQTCC----GSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF 209
Cdd:cd14038  156 QGSLCtsfvGTLQYLAPELLEQQKYTVT-VDYWSFGTLAFECITGFRPF 203
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
15-262 2.61e-24

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: 103.27  E-value: 2.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKimdKNTLGSDLPRIKT----EIEALKNLRHQHICQLYHVLETANKIFMVLEY-- 88
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAMK---KIRLESEEEGVPStairEISLLKELQHPNIVCLEDVLMQENRLYLVFEFls 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG--NKDYHLQ 166
Cdd:cd07861   83 MDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGL-ARAFGipVRVYTHE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCcgSLAYAAPELIQGKSYLGSEADVWSMGIlLYVLMCGFLP-FDDDNVMALYKKIMRG------------------KYD 227
Cdd:cd07861  162 VV--TLWYRAPEVLLGSPRYSTPVDIWSIGT-IFAEMATKKPlFHGDSEIDQLFRIFRIlgtptediwpgvtslpdyKNT 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 375493532 228 VPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07861  239 FPKWkkgslrtavknLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
11-262 3.11e-24

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: 102.84  E-value: 3.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKimdKNTLGSDLPRIKT----EIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIK---KFVESEDDPVIKKialrEIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd07847   80 EYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 tCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCG--FLPFDDDnVMALYK-------------------KIMRG- 224
Cdd:cd07847  160 -YVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGqpLWPGKSD-VDQLYLirktlgdliprhqqifstnQFFKGl 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 225 -----------KYDVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07847  238 sipepetreplESKFPN-ISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
11-279 3.31e-24

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: 103.98  E-value: 3.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKimdKNTLGSDLP----RIKTEIEALKNLRHQHICQLYHVLETANK----- 81
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIK---KIPNAFDVVttakRTLRELKILRHFKHDNIIAIRDILRPKVPyadfk 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 -IFMVLEYCPGgELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG----LCAK 156
Cdd:cd07855   84 dVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmargLCTS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDY---HLQTccgsLAYAAPELIQGKSYLGSEADVWSMG---------------------ILLYVLMCGFLPFD-- 210
Cdd:cd07855  163 PEEHKYFmteYVAT----RWYRAPELMLSLPEYTQAIDMWSVGcifaemlgrrqlfpgknyvhqLQLILTVLGTPSQAvi 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 211 ----DDNVMAL-----------YKKIMRGKydvpkwlSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQS 275
Cdd:cd07855  239 naigADRVRRYiqnlpnkqpvpWETLYPKA-------DQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDC 311

                 ....
gi 375493532 276 KNPF 279
Cdd:cd07855  312 APPF 315
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
11-262 3.44e-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: 102.90  E-value: 3.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKimdKNTLGSDLPRIKT----EIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALK---RVRLDDDDEGVPSsalrEICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCpGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG--NKDY 163
Cdd:cd07839   79 EYC-DQDLKKYFDScNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGL-ARAFGipVRCY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLP-------------------------------FDDD 212
Cdd:cd07839  157 SAEVV--TLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPlfpgndvddqlkrifrllgtpteeswpgvskLPDY 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 213 NVMALYKKIMRGKYDVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07839  235 KPYPMYPATTSLVNVVPK-LNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
11-262 3.98e-24

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 102.97  E-value: 3.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKT-EIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIrEISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 pGGELFDYIISQDRLSEEET--RVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLcAKPKGNKDYHLQ 166
Cdd:PLN00009  84 -DLDLKKHMDSSPDFAKNPRliKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGL-ARAFGIPVRTFT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGIlLYVLMCGFLP-FDDDNVMALYKKIMR------------------GKYD 227
Cdd:PLN00009 162 HEVVTLWYRAPEILLGSRHYSTPVDIWSVGC-IFAEMVNQKPlFPGDSEIDELFKIFRilgtpneetwpgvtslpdYKSA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 375493532 228 VPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:PLN00009 241 FPKWppkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
17-251 5.54e-24

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: 102.30  E-value: 5.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKI-----FMVLEYCPG 91
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENL-LFDEYHKL--KLIDFGLCakpkgnKDYHL 165
Cdd:cd14039   81 GDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIvLQEINGKIvhKIIDLGYA------KDLDQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCC----GSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF----------------DDDNVMALYKkiMRGK 225
Cdd:cd14039  155 GSLCtsfvGTLQYLAPELFENKSYTVT-VDYWSFGTMVFECIAGFRPFlhnlqpftwhekikkkDPKHIFAVEE--MNGE 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 375493532 226 Y----DVPKWLSPSSILL------LQQMLQVDPKKR 251
Cdd:cd14039  232 VrfstHLPQPNNLCSLIVepmegwLQLMLNWDPVQR 267
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
15-265 6.01e-24

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: 102.07  E-value: 6.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06641   10 EKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgNKDYHLQTCCGSLAY 174
Cdd:cd06641   90 LD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT-DTQIKRN*FVGTPFW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALY-------KKIMRGKYdvpkwlSPSSILLLQQMLQVD 247
Cdd:cd06641  168 MAPEVIKQSAY-DSKADIWSLGITAIELARGEPPHSELHPMKVLflipknnPPTLEGNY------SKPLKEFVEACLNKE 240
                        250
                 ....*....|....*...
gi 375493532 248 PKKRISMKNLLNHPWIMQ 265
Cdd:cd06641  241 PSFRPTAKELLKHKFILR 258
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
15-266 6.09e-24

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: 102.05  E-value: 6.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgNKDYHLQTCCGSLAY 174
Cdd:cd06640   90 LD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLT-DTQIKRNTFVGTPFW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDdnvmalyKKIMRGKYDVPKWLSPSSI--------LLLQQMLQV 246
Cdd:cd06640  168 MAPEVIQQSAY-DSKADIWSLGITAIELAKGEPPNSD-------MHPMRVLFLIPKNNPPTLVgdfskpfkEFIDACLNK 239
                        250       260
                 ....*....|....*....|
gi 375493532 247 DPKKRISMKNLLNHPWIMQD 266
Cdd:cd06640  240 DPSFRPTAKELLKHKFIVKN 259
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
17-258 6.89e-24

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: 101.58  E-value: 6.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAcHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELfd 96
Cdd:cd14066    1 IGSGGFGTVYKG-VLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 yiisQDRLSEEETRVVF---------RQIVSAVAYVHSQGY---AHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDY 163
Cdd:cd14066   78 ----EDRLHCHKGSPPLpwpqrlkiaKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLArLIPPSESVS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMCGFLPFDD-----------DNVMALYKKIMRGKYDV-PKW 231
Cdd:cd14066  154 KTSAVKGTIGYLAPEYIRTGRVS-TKSDVYSFGVVLLELLTGKPAVDEnrenasrkdlvEWVESKGKEELEDILDKrLVD 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 232 LSPSSILLLQQMLQV-------DPKKRISMKNLL 258
Cdd:cd14066  233 DDGVEEEEVEALLRLallctrsDPSLRPSMKEVV 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
17-260 7.77e-24

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: 100.65  E-value: 7.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAChiLTGEMVAIKIMDKNTlgsdlpriKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14059    1 LGSGAQGAVFLGK--FRGEEVAVKKVRDEK--------ETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGNKDYHLqTCCGSLAYAA 176
Cdd:cd14059   71 VLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTS-KELSEKSTKM-SFAGTVAWMA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 177 PELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMAlykkIMRG------KYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd14059  149 PEVIRNEP-CSEKVDIWSFGVVLWELLTGEIPYKDVDSSA----IIWGvgsnslQLPVPSTCPDGFKLLMKQCWNSKPRN 223
                        250
                 ....*....|
gi 375493532 251 RISMKNLLNH 260
Cdd:cd14059  224 RPSFRQILMH 233
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
11-252 7.83e-24

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: 101.64  E-value: 7.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVkLACHI-LTGEMVAIKIMDKNtlgsdlpRIK---------TEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05630    2 FRQYRVLGKGGFGEV-CACQVrATGKMYACKKLEKK-------RIKkrkgeamalNEKQILEKVNSRFVVSLAYAYETKD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-P 157
Cdd:cd05630   74 ALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFyaAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHvP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKdyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNvmalyKKIMR---------GKYDV 228
Cdd:cd05630  154 EGQT---IKGRVGTVGYMAPEVVKNERYTFS-PDWWALGCLLYEMIAGQSPFQQRK-----KKIKReeverlvkeVPEEY 224
                        250       260
                 ....*....|....*....|....
gi 375493532 229 PKWLSPSSILLLQQMLQVDPKKRI 252
Cdd:cd05630  225 SEKFSPQARSLCSMLLCKDPAERL 248
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
55-259 9.78e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 104.71  E-value: 9.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  55 KTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIisQDRLSEE------ETRVVFRQIVSAVAYVHSQGY 128
Cdd:PTZ00267 113 RSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQI--KQRLKEHlpfqeyEVGLLFYQIVLALDEVHSRKM 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 129 AHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC-CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFL 207
Cdd:PTZ00267 191 MHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSfCGTPYYLAPELWERKRY-SKKADMWSLGVILYELLTLHR 269
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 208 PFDDDNVMALYKKIMRGKYD-VPKWLSPSSILLLQQMLQVDPKKRISMKNLLN 259
Cdd:PTZ00267 270 PFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLH 322
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
4-262 1.26e-23

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: 101.24  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   4 YDELLKYYELhETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKI 82
Cdd:cd07871    1 FGKLETYVKL-DKLGEGTYATVFKGRSKLTENLVALKeIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIIHTERCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGgELFDYIISQDRL-SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGN 160
Cdd:cd07871   79 TLVFEYLDS-DLKQYLDNCGNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLArAKSVPT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR----------------- 223
Cdd:cd07871  158 KTYSNEVV--TLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRllgtpteetwpgvtsne 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 224 --GKYDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07871  236 efRSYLFPQYraqplinhaprLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
66-261 1.42e-23

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: 100.42  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  66 HQHICQLYHVLETANKIFMVLEYCPGgELFDYIISQD------RLSEEETRVVfRQIVSAVAYVHSQGYAHRDLKPENLL 139
Cdd:cd13982   54 HPNVIRYFCTEKDRQFLYIALELCAA-SLQDLVESPResklflRPGLEPVRLL-RQIASGLAHLHSLNIVHRDLKPQNIL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 140 F--DEYH---KLKLIDFGLCAKPKGNKD--YHLQTCCGSLAYAAPELIQGKSYLGSEA--DVWSMG-ILLYVLMCGFLPF 209
Cdd:cd13982  132 IstPNAHgnvRAMISDFGLCKKLDVGRSsfSRRSGVAGTSGWIAPEMLSGSTKRRQTRavDIFSLGcVFYYVLSGGSHPF 211
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 210 DDDnvmalYKK---IMRGKYDVPKWLS-----PSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd13982  212 GDK-----LEReanILKGKYSLDKLLSlgehgPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
17-225 1.48e-23

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: 100.22  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG--- 92
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKaLLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGslk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSeeetrVVFR---QIVSAVAYVH--SQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG-----NKD 162
Cdd:cd13978   81 SLLEREIQDVPWS-----LRFRiihEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGL-SKLGMksisaNRR 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKSYLGSEA-DVWSMGILLYVLMCGFLPFDDDNVMALykkIMRGK 225
Cdd:cd13978  155 RGTENLGGTPIYMAPEAFDDFNKKPTSKsDVYSFAIVIWAVLTRKEPFENAINPLL---IMQIV 215
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
15-262 1.92e-23

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: 100.81  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL-GSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGgE 93
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEeGVPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQ-DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYHLQTCcgS 171
Cdd:cd07870   84 LAQYMIQHpGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLArAKSIPSQTYSSEVV--T 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 LAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMR-----------GKYDVPK----WLSPS 235
Cdd:cd07870  162 LWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTvlgvptedtwpGVSKLPNykpeWFLPC 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 236 SILLL-----------------QQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07870  242 KPQQLrvvwkrlsrppkaedlaSQMLMMFPKDRISAQDALLHPY 285
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
15-265 2.09e-23

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: 100.13  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06642   10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKgNKDYHLQTCCGSLAY 174
Cdd:cd06642   90 LD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLT-DTQIKRNTFVGTPFW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVmalykkiMRGKYDVPKwLSPSSIL---------LLQQMLQ 245
Cdd:cd06642  168 MAPEVIKQSAY-DFKADIWSLGITAIELAKGEPPNSDLHP-------MRVLFLIPK-NSPPTLEgqhskpfkeFVEACLN 238
                        250       260
                 ....*....|....*....|
gi 375493532 246 VDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06642  239 KDPRFRPTAKELLKHKFITR 258
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
54-261 2.11e-23

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: 99.74  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  54 IKTEIEALKNLRHQHICQLYHVLET------ANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQG 127
Cdd:cd14012   45 LEKELESLKKLRHPNLVSYLAFSIErrgrsdGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 128 YAHRDLKPENLLFDEYH---KLKLIDFGLCAKP-----KGNKDYHLQTCcgslaYAAPELIQGKSYLGSEADVWSMGILL 199
Cdd:cd14012  125 VVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLldmcsRGSLDEFKQTY-----WLPPELAQGSKSPTRKTDVWDLGLLF 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375493532 200 YVLMCGFLPFDDDNVMALYKkimrgkydVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14012  200 LQMLFGLDVLEKYTSPNPVL--------VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
6-279 2.50e-23

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: 101.66  E-value: 2.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   6 ELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDK--NTLgSDLPRIKTEIEALKNLRHQHICQLYHV------LE 77
Cdd:cd07878   12 EVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSL-IHARRTYRELRLLKHMKHENVIGLLDVftpatsIE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  78 TANKIFMVLEYCpGGELfDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKp 157
Cdd:cd07878   91 NFNEVYLVTNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 kgnKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-------------- 223
Cdd:cd07878  168 ---ADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtpspevlkkis 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493532 224 ----GKY-------------DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQdYNYPVEWQSKNPF 279
Cdd:cd07878  245 sehaRKYiqslphmpqqdlkKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQ-YHDPEDEPEAEPY 316
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
9-266 2.80e-23

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 101.38  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKT-------------EIEALKNLRHQHICQLYHV 75
Cdd:PTZ00024   9 RYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  76 LETANKIFMVLEYCpGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA 155
Cdd:PTZ00024  89 YVEGDFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLAR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 K-------PKGNKDYHLQ------TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKI- 221
Cdd:PTZ00024 168 RygyppysDTLSKDETMQrreemtSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIf 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375493532 222 -MRGKYDVPKW--------------------------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:PTZ00024 248 eLLGTPNEDNWpqakklplyteftprkpkdlktifpnASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSD 319
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
11-261 2.88e-23

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: 99.31  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKrSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CpGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTc 168
Cdd:cd14050   83 C-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQE- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 cGSLAYAAPELIQGKsyLGSEADVWSMGILLYVLMCGF-LPFDDDnvmaLYKKIMRGkyDVP----KWLSPSSILLLQQM 243
Cdd:cd14050  161 -GDPRYMAPELLQGS--FTKAADIFSLGITILELACNLeLPSGGD----GWHQLRQG--YLPeeftAGLSPELRSIIKLM 231
                        250
                 ....*....|....*...
gi 375493532 244 LQVDPKKRISMKNLLNHP 261
Cdd:cd14050  232 MDPDPERRPTAEDLLALP 249
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
8-262 2.90e-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: 100.46  E-value: 2.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKeIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIIHTEKSLTLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCpGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYH 164
Cdd:cd07873   80 EYL-DKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLArAKSIPTKTYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-------------------GK 225
Cdd:cd07873  159 NEVV--TLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRilgtpteetwpgilsneefKS 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 375493532 226 YDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07873  237 YNYPKYradalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
11-262 2.94e-23

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: 100.29  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKI----MDKNTLGSDLPRiktEIEALKNLRHQ-HICQLYHVLETANK---- 81
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKtrleMEEEGVPSTALR---EVSLLQMLSQSiYIVRLLDVEHVEENgkpl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCpGGELFDYIISQDR-----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLC- 154
Cdd:cd07837   80 LYLVFEYL-DTDLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLGr 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVL--MCGFLPFDDD--NVMALYK----------- 219
Cdd:cd07837  159 AFTIPIKSYTHEIV--TLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMsrKQPLFPGDSElqQLLHIFRllgtpneevwp 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 220 --KIMRGKYDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07837  237 gvSKLRDWHEYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
9-285 3.38e-23

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: 101.18  E-value: 3.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELhETIGTGGFAKVKLACHILTGEMVAIKIMDKnTLGSDL--PRIKTEIEALKNLRHQHICQLYHV------LETAN 80
Cdd:cd07880   16 RYRDL-KQVGSGAYGTVCSALDRRTGAKVAIKKLYR-PFQSELfaKRAYRELRLLKHMKHENVIGLLDVftpdlsLDRFH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCpgGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgn 160
Cdd:cd07880   94 DFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ---- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR----------------- 223
Cdd:cd07880  168 TDSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKvtgtpskefvqklqsed 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 224 -----------GKYDVPKWL---SPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKnPFIHLDDD 285
Cdd:cd07880  248 aknyvkklprfRKKDFRSLLpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETEAP-PYDDSFDE 322
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
11-262 4.30e-23

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 99.74  E-value: 4.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVkLACHI-LTGEMVAIKIMDKNtlgsdlpRIK---------TEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05605    2 FRQYRVLGKGGFGEV-CACQVrATGKMYACKKLEKK-------RIKkrkgeamalNEKQILEKVNSRFVVSLAYAYETKD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPK 158
Cdd:cd05605   74 ALCLVLTIMNGGDLKFHIYNMGNPGFEEERAVFyaAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTccGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFdddnvMALYKKIMRG------KYDVPKW- 231
Cdd:cd05605  154 EGETIRGRV--GTVGYMAPEVVKNERYTFS-PDWWGLGCLIYEMIEGQAPF-----RARKEKVKREevdrrvKEDQEEYs 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 232 --LSPSSILLLQQMLQVDPKKRI-----SMKNLLNHPW 262
Cdd:cd05605  226 ekFSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPF 263
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
6-307 8.05e-23

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: 100.11  E-value: 8.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   6 ELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKnTLGSDL--PRIKTEIEALKNLRHQHICQLYHV------LE 77
Cdd:cd07877   14 EVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSR-PFQSIIhaKRTYRELRLLKHMKHENVIGLLDVftparsLE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  78 TANKIFMVlEYCPGGELfDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkp 157
Cdd:cd07877   93 EFNDVYLV-THLMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR-- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 kgNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-------------- 223
Cdd:cd07877  169 --HTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRlvgtpgaellkkis 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 224 ---------GKYDVPKW--------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQdYNYPVEWQSKNPFihldddc 286
Cdd:cd07877  247 sesarnyiqSLTQMPKMnfanvfigANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ-YHDPDDEPVADPY------- 318
                        330       340
                 ....*....|....*....|....*..
gi 375493532 287 vtELSVHHRN------NRQTMEDLISL 307
Cdd:cd07877  319 --DQSFESRDllidewKSLTYDEVISF 343
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
5-297 1.09e-22

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: 99.55  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLR-HQHICQLYHVLETANK- 81
Cdd:cd07852    3 KHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRAENDk 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 -IFMVleycpggelFDYI-------ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd07852   83 dIYLV---------FEYMetdlhavIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 C------AKPKGNK---DYhlqtccgsLA---YAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKI 221
Cdd:cd07852  154 ArslsqlEEDDENPvltDY--------VAtrwYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKI 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 222 MR-----GKYDVPKWLSP--SSIL------------------------LLQQMLQVDPKKRISMKNLLNHPWIMQDYNYP 270
Cdd:cd07852  226 IEvigrpSAEDIESIQSPfaATMLeslppsrpksldelfpkaspdaldLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPA 305
                        330       340
                 ....*....|....*....|....*....
gi 375493532 271 VEWQSKNPF-IHLDDDcvTELSVH-HRNN 297
Cdd:cd07852  306 DEPSLPGPIvIPLDDN--KKLTVDeYRNR 332
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
17-289 1.10e-22

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: 99.37  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDK---NTLgsDLPRIKTEIEALKNLRHQHICQLYHVL-----ETANKIFMVLEY 88
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIANafdNRI--DAKRTLREIKLLRHLDHENVIAIKDIMppphrEAFNDVYIVYEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CpGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTC 168
Cdd:cd07858   91 M-DTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL-ARTTSEKGDFMTEY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLM-----------------------------CGFLpfDDDNV----- 214
Cdd:cd07858  169 VVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLgrkplfpgkdyvhqlklitellgspseedLGFI--RNEKArryir 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 215 -MALYKKI-MRGKYdvPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPF-IHLDDDCVTE 289
Cdd:cd07858  247 sLPYTPRQsFARLF--PH-ANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTPFsFDFEEDALTE 321
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
11-262 1.19e-22

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: 98.98  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK--IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANK------- 81
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKkvLMENEKEGFPITALR-EIKILQLLKHENVVNLIEICRTKATpynrykg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 -IFMVLEYCPG--GELFDYIisQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC---A 155
Cdd:cd07865   93 sIYLVFEFCEHdlAGLLSNK--NVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLArafS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILL------YVLM---------------CG-FLPFDDDN 213
Cdd:cd07865  171 LAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMaemwtrSPIMqgnteqhqltlisqlCGsITPEVWPG 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 214 V--MALYKKIM--RGKYDV------PKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07865  251 VdkLELFKKMElpQGQKRKvkerlkPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
15-209 1.21e-22

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: 100.09  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL--GSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVlnRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK----------PKGN-- 160
Cdd:cd05626   87 DMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGfrwthnskyyQKGShi 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 ------------------------------KDYHlQTC-----CGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMCG 205
Cdd:cd05626  167 rqdsmepsdlwddvsncrcgdrlktleqraTKQH-QRClahslVGTPNYIAPEVLLRKGYT-QLCDWWSVGVILFEMLVG 244

                 ....
gi 375493532 206 FLPF 209
Cdd:cd05626  245 QPPF 248
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
11-263 1.22e-22

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: 98.16  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgSDLPRIKTEIEALKNL-RHQHICQLYHVLETA------NKIF 83
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE--DEEEEIKLEINMLKKYsHHRNIATYYGAFIKKsppghdDQLW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPK 158
Cdd:cd06636   96 LVMEFCGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAqldRTV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDyhlqTCCGSLAYAAPELI----QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKW 231
Cdd:cd06636  176 GRRN----TFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpppKLKSKKW 251
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 232 lSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06636  252 -SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
17-258 1.25e-22

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: 98.08  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLaCHI-----LTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVL--ETANKIFMVLEYC 89
Cdd:cd05079   12 LGEGHFGKVEL-CRYdpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICteDGGNGIKLIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYII-SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHL--Q 166
Cdd:cd05079   91 PSGSLKEYLPrNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTvkD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPE-LIQGKSYLGSeaDVWSMGILLYVLM--CGflpfDDDNVMALYKKIM---RGKYDVPKWLS------- 233
Cdd:cd05079  171 DLDSPVFWYAPEcLIQSKFYIAS--DVWSFGVTLYELLtyCD----SESSPMTLFLKMIgptHGQMTVTRLVRvleegkr 244
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 234 -------PSSIL-LLQQMLQVDPKKRISMKNLL 258
Cdd:cd05079  245 lprppncPEEVYqLMRKCWEFQPSKRTTFQNLI 277
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
8-257 1.35e-22

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: 97.36  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHilTGEMVAIKIMDKNTLGSDLpriKTEIEALKNLRHQHICQLYHVL-ETANKIFMVL 86
Cdd:cd05082    5 MKELKLLQTIGKGEFGDVMLGDY--RGNKVAVKCIKNDATAQAF---LAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyh 164
Cdd:cd05082   80 EYMAKGSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQD-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 lqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQ 242
Cdd:cd05082  158 --TGKLPVKWTAPEALREKKF-STKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPRVEKGyKMDAPDGCPPAVYDVMKN 234
                        250
                 ....*....|....*
gi 375493532 243 MLQVDPKKRISMKNL 257
Cdd:cd05082  235 CWHLDAAMRPSFLQL 249
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
11-268 1.60e-22

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: 98.25  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDknTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETAN------KIF 83
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD--VTGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNppgmddQLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA---KPK 158
Cdd:cd06637   86 LVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAqldRTV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDyhlqTCCGSLAYAAPELI----QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVPKW 231
Cdd:cd06637  166 GRRN----TFIGTPYWMAPEVIacdeNPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpapRLKSKKW 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 375493532 232 lSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYN 268
Cdd:cd06637  242 -SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPN 277
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
9-211 1.63e-22

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: 98.05  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVklaCHIL---TGEMVAIKIMDKNTL----GSDLPRIKTEIeaLKNLRHQHICQLYHVLETANK 81
Cdd:cd05607    2 KYFYEFRVLGKGGFGEV---CAVQvknTGQMYACKKLDKKRLkkksGEKMALLEKEI--LEKVNSPFIVSLAYAFETKTH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG 159
Cdd:cd05607   77 LCLVMSLMNGGDLKYHIYNVGERGIEMERVIFysAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 160 NKDyhLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDD 211
Cdd:cd05607  157 GKP--ITQRAGTNGYMAPEILKEESY-SYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
11-285 3.93e-22

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: 97.76  E-value: 3.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIM---DKNTLGSdlpRIKTEIEALKNLRHQHICQLYHVL-----ETANKI 82
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfEHQTYCL---RTLREIKILLRFKHENIIGILDIQrpptfESFKDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGgELFDYIISQDrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC--AKPKGN 160
Cdd:cd07849   84 YIVQELMET-DLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAriADPEHD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPE-LIQGKSYLGSeADVWSMG-ILLYVLMC-----------------GFL--PFDDD-----NV 214
Cdd:cd07849  162 HTGFLTEYVATRWYRAPEiMLNSKGYTKA-IDIWSVGcILAEMLSNrplfpgkdylhqlnlilGILgtPSQEDlnciiSL 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 215 MAL--------YKKIMRGKYdVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDD 285
Cdd:cd07849  241 KARnyikslpfKPKVPWNKL-FPN-ADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMEL 317
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
17-258 4.23e-22

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: 95.92  E-value: 4.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMD---KNTLGSDLPRIKTEIEALKNLRHQHICQLYHV-LETANkIFMVLEYCPGG 92
Cdd:cd14061    2 IGVGGFGKVYRG--IWRGEEVAVKAARqdpDEDISVTLENVRQEARLFWMLRHPNIIALRGVcLQPPN-LCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELfDYIISQDRLSEEetrVVFR---QIVSAVAYVHSQG---YAHRDLKPENLLFDE--------YHKLKLIDFGLCakpk 158
Cdd:cd14061   79 AL-NRVLAGRKIPPH---VLVDwaiQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLA---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 gnKDYHLQT---CCGSLAYAAPELIQGKSYlgSEA-DVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPkwlSP 234
Cdd:cd14061  151 --REWHKTTrmsAAGTYAWMAPEVIKSSTF--SKAsDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTLP---IP 223
                        250       260
                 ....*....|....*....|....*....
gi 375493532 235 SSI-----LLLQQMLQVDPKKRISMKNLL 258
Cdd:cd14061  224 STCpepfaQLMKDCWQPDPHDRPSFADIL 252
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
11-209 4.25e-22

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 97.35  E-value: 4.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVkLACHI-LTGEMVAIKIMDKNtlgsdlpRIK---------TEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05632    4 FRQYRVLGKGGFGEV-CACQVrATGKMYACKRLEKK-------RIKkrkgesmalNEKQILEKVNSQFVVNLAYAYETKD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-P 157
Cdd:cd05632   76 ALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFyaAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKiP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 158 KGNKdyhLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd05632  156 EGES---IRGRVGTVGYMAPEVLNNQRY-TLSPDYWGLGCLIYEMIEGQSPF 203
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-262 4.87e-22

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: 95.74  E-value: 4.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRikTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14108    3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSAR--RELALLAELDHKSIVRFHDAFEKRRVVIIVTELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDyIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHKLKLIDFGLCAKPKGNKDYHLQT 167
Cdd:cd14108   81 HEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQYCKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 ccGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPF----DDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQM 243
Cdd:cd14108  160 --GTPEFVAPEIVN-QSPVSKVTDIWPVGVIAYLCLTGISPFvgenDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKV 236
                        250
                 ....*....|....*....
gi 375493532 244 LqVDPKKRISMKNLLNHPW 262
Cdd:cd14108  237 L-VSDRLRPDAEETLEHPW 254
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
17-260 5.12e-22

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: 95.64  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKImdkNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE---LKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLK---LIDFGLCAK------PKGNKDYHLQ 166
Cdd:cd14065   78 LLKSMDEQLPWSQRVSLaKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREmpdektKKPDRKKRLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TcCGSLAYAAPELIQGKSYLGsEADVWSMGILLYVLMcGFLPFDDDNVmalyKKIMRGKYDVPKWLS------PSSILLL 240
Cdd:cd14065  158 V-VGSPYWMAPEMLRGESYDE-KVDVFSFGIVLCEII-GRVPADPDYL----PRTMDFGLDVRAFRTlyvpdcPPSFLPL 230
                        250       260
                 ....*....|....*....|.
gi 375493532 241 Q-QMLQVDPKKRISMKNLLNH 260
Cdd:cd14065  231 AiRCCQLDPEKRPSFVELEHH 251
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
9-263 5.13e-22

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: 97.26  E-value: 5.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELhETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHV-LETANKIFMVL 86
Cdd:cd07856   11 RYSDL-QPVGMGAFGLVCSARDQLTGQNVAVKkIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCpgGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnKDYHLQ 166
Cdd:cd07856   90 ELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI----QDPQMT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCG--FLPFDD-------------------------DNVMALYK 219
Cdd:cd07856  164 GYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGkpLFPGKDhvnqfsiitellgtppddvinticsENTLRFVQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 220 KIMRgKYDVP-----KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07856  244 SLPK-RERVPfsekfKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
9-203 5.25e-22

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: 96.51  E-value: 5.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHIL----TGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANK--I 82
Cdd:cd05080    4 RYLKKIRDLGEGHFGKVSLYCYDPtndgTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNK 161
Cdd:cd05080   84 QLIMEYVPLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAkAVPEGHE 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 375493532 162 DYHLQTCCGS--LAYAAPELIQGKSYLGSeaDVWSMGILLYVLM 203
Cdd:cd05080  163 YYRVREDGDSpvFWYAPECLKEYKFYYAS--DVWSFGVTLYELL 204
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
3-260 5.56e-22

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: 95.88  E-value: 5.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   3 DYDELLkyyeLHETIGTGGFAKVKLAchILTGEMVAIKIMDKN---TLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA 79
Cdd:cd14145    4 DFSELV----LEEIIGIGGFGKVYRA--IWIGDEVAVKAARHDpdeDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELfDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYA---HRDLKPENLLF-------DEYHK-LKL 148
Cdd:cd14145   78 PNLCLVMEFARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvengDLSNKiLKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLCakpkgnKDYHLQT---CCGSLAYAAPELIQGkSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd14145  157 TDFGLA------REWHRTTkmsAAGTYAWMAPEVIRS-SMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 375493532 226 YDVPkwlSPSSI-----LLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd14145  230 LSLP---IPSTCpepfaRLMEDCWNPDPHSRPPFTNILDQ 266
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
11-263 6.49e-22

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: 96.41  E-value: 6.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKI--MDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVL----------ET 78
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKvrLDNEKEGFPITAIR-EIKILRQLNHRSVVNLKEIVtdkqdaldfkKD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPG---GELFDYIISqdrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC- 154
Cdd:cd07864   88 KGAFYLVFEYMDHdlmGLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLAr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 ------AKPKGNKDYhlqtccgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR--GKY 226
Cdd:cd07864  165 lynseeSRPYTNKVI-------TLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRlcGSP 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 227 DVPKW----------------------------LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07864  238 CPAVWpdviklpyfntmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
15-218 6.81e-22

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: 95.53  E-value: 6.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAchILTGEMVAIKIMD---KNTLGSDLPRikTEIEALkNLRHQHICQLY---HVLETANKIFMVLEY 88
Cdd:cd13979    9 EPLGSGGFGSVYKA--TYKGETVAVKIVRrrrKNRASRQSFW--AELNAA-RLRHENIVRVLaaeTGTDFASLGLIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYII-SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-PKGN-KDYHL 165
Cdd:cd13979   84 CGNGTLQQLIYeGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKlGEGNeVGTPR 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 166 QTCCGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALY 218
Cdd:cd13979  164 SHIGGTYTYRAPELLKGER-VTPKADIYSFGITLWQMLTRELPYAGLRQHVLY 215
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
11-263 8.31e-22

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 95.85  E-value: 8.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgsdLPRIKTEIEA----LKNLR-HQHICQLYHV-----LETAN 80
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDP------IHDIDEEIEAeyniLKALSdHPNVVKFYGMyykkdVKNGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFD----YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd06638   94 QLWLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKdYHLQTCCGSLAYAAPELIQGKSYLGS----EADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---KYDVP 229
Cdd:cd06638  174 LTSTR-LRRNTSVGTPFWMAPEVIACEQQLDStydaRCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppTLHQP 252
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 230 KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06638  253 ELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
5-262 1.08e-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: 96.48  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNtlgsdLPRI----KTEIEALKNLRHQ------HICQLYH 74
Cdd:cd14134    8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII-RN-----VEKYreaaKIEIDVLETLAEKdpngksHCVQLRD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  75 VLETANKIFMVLEYCpGGELFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF--DEYHK----- 145
Cdd:cd14134   82 WFDYRGHMCIVFELL-GPSLYDFLKKNNygPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdSDYVKvynpk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 146 ------------LKLIDFGLCAKpkgNKDYHlqtccGSLA----YAAPELIQGksyLG-SE-ADVWSMGILLYVLMCGFL 207
Cdd:cd14134  161 kkrqirvpkstdIKLIDFGSATF---DDEYH-----SSIVstrhYRAPEVILG---LGwSYpCDVWSIGCILVELYTGEL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 208 PFDD-DNV--MALYKKIM--------------------------------RGKY--DVPKWLSPSSIL----------LL 240
Cdd:cd14134  230 LFQThDNLehLAMMERILgplpkrmirrakkgakyfyfyhgrldwpegssSGRSikRVCKPLKRLMLLvdpehrllfdLI 309
                        330       340
                 ....*....|....*....|..
gi 375493532 241 QQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14134  310 RKMLEYDPSKRITAKEALKHPF 331
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
17-209 1.09e-21

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: 96.02  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHV---LETANKIfMVLEYCPGGE 93
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIeeeLTTRHKV-LVMELCPCGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKLKLIDFGlcAKPKGNKDYHLQ 166
Cdd:cd13988   80 LYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFG--AARELEDDEQFV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 167 TCCGSLAYAAPELIQ--------GKSYlGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd13988  158 SLYGTEEYLHPDMYEravlrkdhQKKY-GATVDLWSIGVTFYHAATGSLPF 207
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
15-265 1.24e-21

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: 95.33  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd06619    7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYiisqDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKdyhLQTCCGSLAY 174
Cdd:cd06619   87 DVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSI---AKTYVGTNAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF-----DDDNVMALYKKIMRGKYDVPKW----LSPSSILLLQQMLQ 245
Cdd:cd06619  160 MAPERISGEQY-GIHSDVWSLGISFMELALGRFPYpqiqkNQGSLMPLQLLQCIVDEDPPVLpvgqFSEKFVHFITQCMR 238
                        250       260
                 ....*....|....*....|
gi 375493532 246 VDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06619  239 KQPKERPAPENLMDHPFIVQ 258
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
9-262 1.42e-21

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 97.80  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNtlgsdlPRIKT-EIEALKNLRHQHICQL--YHVLETANK---- 81
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQD------PQYKNrELLIMKNLNHINIIFLkdYYYTECFKKnekn 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFM--VLEYCPGgELFDYIISQDRLSEEETRVVFR----QIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLC 154
Cdd:PTZ00036 140 IFLnvVMEFIPQ-TVHKYMKHYARNNHALPLFLVKlysyQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSA 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDYHLQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDD----DNVMALYK----------K 220
Cdd:PTZ00036 219 KNLLAGQRSVSYIC--SRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGqssvDQLVRIIQvlgtptedqlK 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 221 IMRGKY------DV---------PKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:PTZ00036 297 EMNPNYadikfpDVkpkdlkkvfPKGTPDDAINFISQFLKYEPLKRLNPIEALADPF 353
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
17-274 1.51e-21

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: 94.81  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNtlgsdlpRIKT---EIEALkNLRHQ-----------HICQLYHVLETANKI 82
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKK-------RIKMkqgETLAL-NERIMlslvstggdcpFIVCMTYAFQTPDKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD 162
Cdd:cd05606   74 CFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YhlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVM---ALYKKIMRGKYDVPKWLSPSSILL 239
Cdd:cd05606  154 H---ASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKdkhEIDRMTLTMNVELPDSFSPELKSL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 375493532 240 LQQMLQVDPKKRI-----SMKNLLNHPWIMQdynypVEWQ 274
Cdd:cd05606  231 LEGLLQRDVSKRLgclgrGATEVKEHPFFKG-----VDWQ 265
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
9-263 2.22e-21

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: 93.83  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL- 86
Cdd:cd13983    1 RYLKFNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKaERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 -EYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGY--AHRDLKPENLLFDEYH-KLKLIDFGLCAKPKGNKD 162
Cdd:cd13983   81 tELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPpiIHRDLKCDNIFINGNTgEVKIGDLGLATLLRQSFA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YhlqTCCGSLAYAAPELIQGKsYlGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRGKYdvPKWLSPSSILLLQ 241
Cdd:cd13983  161 K---SVIGTPEFMAPEMYEEH-Y-DEKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSGIK--PESLSKVKDPELK 233
                        250       260
                 ....*....|....*....|....*
gi 375493532 242 QMLQ---VDPKKRISMKNLLNHPWI 263
Cdd:cd13983  234 DFIEkclKPPDERPSARELLEHPFF 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
17-250 2.62e-21

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: 94.43  E-value: 2.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM---DKNTLGSDLPRiktEIEALKNLRHQHICQLYHV-LETANKIFMVLEYCPGG 92
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSVRKQILR---ELQILHECHSPYIVSFYGAfLNENNNIIICMEYMDCG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELfDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGY-AHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnkdyhL----- 165
Cdd:cd06620   90 SL-DKILKKKGpFPEEVLGKIAVAVLEGLTYLYNVHRiIHRDIKPSNILVNSKGQIKLCDFGVSGE--------Linsia 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVmalykkimrgkyDVPKWLSPSSIL-LLQQML 244
Cdd:cd06620  161 DTFVGTSTYMSPERIQGGKY-SVKSDVWSLGLSIIELALGEFPFAGSND------------DDDGYNGPMGILdLLQRIV 227

                 ....*.
gi 375493532 245 QVDPKK 250
Cdd:cd06620  228 NEPPPR 233
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
8-262 2.75e-21

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: 94.67  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKeIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIVHTDKSLTLVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCpGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYH 164
Cdd:cd07872   84 EYL-DKDLKQYMDDcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLArAKSVPTKTYS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-------------------GK 225
Cdd:cd07872  163 NEVV--TLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRllgtpteetwpgissndefKN 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 375493532 226 YDVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07872  241 YNFPKYkpqplinhaprLDTEGIELLTKFLQYESKKRISAEEAMKHAY 288
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-259 3.21e-21

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: 93.57  E-value: 3.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLAchILTGEMVAIKIM--DKNTLGSDLprikTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05039    9 KLGELIGKGEFGDVMLG--DYRGQKVAVKCLkdDSTAAQAFL----AEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDR-LSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPkgnKDYHLQT 167
Cdd:cd05039   83 AKGSLVDYLRSRGRaVITRKDQLGFaLDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGL-AKE---ASSNQDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd05039  159 GKLPIKWTAPEALREKKF-STKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPHVEKGyRMEAPEGCPPEVYKVMKNCWE 237
                        250
                 ....*....|....
gi 375493532 246 VDPKKRISMKNLLN 259
Cdd:cd05039  238 LDPAKRPTFKQLRE 251
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
11-252 3.42e-21

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: 95.13  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL----GSDLP---RIKTEIEALKNLrhQHICQLYHVLETANKIF 83
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkqGETLAlneRIMLSLVSTGDC--PFIVCMTYAFHTPDKLC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd05633   85 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 hlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVM---ALYKKIMRGKYDVPKWLSPSSILLL 240
Cdd:cd05633  165 ---ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPDSFSPELKSLL 241
                        250
                 ....*....|..
gi 375493532 241 QQMLQVDPKKRI 252
Cdd:cd05633  242 EGLLQRDVSKRL 253
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
12-263 6.39e-21

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: 94.81  E-value: 6.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHILTGEMVAIKIMDK---NTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETAN-----KIF 83
Cdd:cd07853    3 EPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNvfqNLVSCK--RVFRELKMLCFFKHDNVLSALDILQPPHidpfeEIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGgELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd07853   81 VVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFD----------------DDNVMALY-------KK 220
Cdd:cd07853  160 HMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQaqspiqqldlitdllgTPSLEAMRsacegarAH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 221 IMRGKYDVP------KWLSPSS---ILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07853  240 ILRGPHKPPslpvlyTLSSQATheaVHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
11-262 6.69e-21

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: 93.53  E-value: 6.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTlgSDLPRIKT--EIEALKNLRHQHICQLYHV--------LETA 79
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNE--KDGFPITAlrEIKILKKLKHPNVVPLIDMaverpdksKRKR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCP---GGELFDYIIsqdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAK 156
Cdd:cd07866   88 GSVYMVTPYMDhdlSGLLENPSV---KLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGL-AR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDYHLQTCCGSLA-----------YAAPELIQGKSYLGSEADVWSMG-----------IL----------LYVLMC 204
Cdd:cd07866  164 PYDGPPPNPKGGGGGGTrkytnlvvtrwYRPPELLLGERRYTTAVDIWGIGcvfaemftrrpILqgksdidqlhLIFKLC 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 205 G-----------FLP-FDDDNVMALYKKIMRGKYdvpKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07866  244 GtpteetwpgwrSLPgCEGVHSFTNYPRTLEERF---GKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
5-271 7.00e-21

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: 93.26  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGtGGFAKVKLAChilTGEMVAIKIM--DKNTlgsDLPR-IKTEIEALKNLRHQHICQLY--HVLETA 79
Cdd:cd06621    1 DKIVELSSLGEGAG-GSVTKCRLRN---TKTIFALKTIttDPNP---DVQKqILRELEINKSCASPYIVKYYgaFLDEQD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELfDYIISQ-----DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC 154
Cdd:cd06621   74 SSIGIAMEYCEGGSL-DSIYKKvkkkgGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AKPKGNKDyhlQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNV-----MALYKKIMRGK---- 225
Cdd:cd06621  153 GELVNSLA---GTFTGTSYYMAPERIQGGPYSIT-SDVWSLGLTLLEVAQNRFPFPPEGEpplgpIELLSYIVNMPnpel 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 226 YDVP----KWlSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPV 271
Cdd:cd06621  229 KDEPengiKW-SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKV 277
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
11-257 7.62e-21

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: 92.50  E-value: 7.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHiLTGEMVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLW-KNRVRVAIKIL-KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTC 168
Cdd:cd05148   86 KGSLLAFLRSPEgqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGL-ARLIKEDVYLSSDK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGkYDVPKWLS-PSSILLLqqMLQ- 245
Cdd:cd05148  165 KIPYKWTAPEAASHGTF-STKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG-YRMPCPAKcPQEIYKI--MLEc 240
                        250
                 ....*....|....
gi 375493532 246 --VDPKKRISMKNL 257
Cdd:cd05148  241 waAEPEDRPSFKAL 254
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
9-265 8.61e-21

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: 92.13  E-value: 8.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:cd06607    2 IFEDLRE-IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTekWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELfDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA--KPKgnkdy 163
Cdd:cd06607   81 EYCLGSAS-DIVeVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASlvCPA----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 hlQTCCGSLAYAAPELI----QGKsYLGsEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKimrGKYDVP-----KWlS 233
Cdd:cd06607  155 --NSFVGTPYWMAPEVIlamdEGQ-YDG-KVDVWSLGITCIELAERKPPLFNMNAMsALYHI---AQNDSPtlssgEW-S 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 234 PSSILLLQQMLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd06607  227 DDFRNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
11-263 1.04e-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: 92.75  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKntlgsdLPRIKTEIEALKNL-----RHQHICQLYHVLETANK---- 81
Cdd:cd06639   24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDP------ISDVDEEIEAEYNIlrslpNHPNVVKFYGMFYKADQyvgg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 -IFMVLEYCPGGELFDYI----ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd06639   98 qLWLVLELCNGGSVTELVkgllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKdYHLQTCCGSLAYAAPELI----QGKSYLGSEADVWSMGILLYVLMCGFLP-FDDDNVMALYKkimrgkydVPKw 231
Cdd:cd06639  178 LTSAR-LRRNTSVGTPFWMAPEVIaceqQYDYSYDARCDVWSLGITAIELADGDPPlFDMHPVKALFK--------IPR- 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 232 lSPSSILL------------LQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06639  248 -NPPPTLLnpekwcrgfshfISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
14-269 1.24e-20

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: 92.36  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  14 HETIGTGGFAKVkLACHI-LTGEMVAIKIMDKNtlgsdlpRIK---------TEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd05631    5 YRVLGKGGFGEV-CACQVrATGKMYACKKLEKK-------RIKkrkgeamalNEKRILEKVNSRFVVSLAYAYETKDALC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK-PKGN 160
Cdd:cd05631   77 LVLTIMNGGDLKFHIYNMGNPGFDEQRAIFyaAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQiPEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KdyhLQTCCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPFDDDNVMALYKKI-MRGKYDVPKW---LSPSS 236
Cdd:cd05631  157 T---VRGRVGTVGYMAPEVINNEKYTFS-PDWWGLGCLIYEMIQGQSPFRKRKERVKREEVdRRVKEDQEEYsekFSEDA 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 237 ILLLQQMLQVDPKKRISMK-----NLLNHPwIMQDYNY 269
Cdd:cd05631  233 KSICRMLLTKNPKERLGCRgngaaGVKQHP-IFKNINF 269
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
17-256 2.98e-20

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: 91.48  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVkLACHI-LTGEMVAIKIMDKNTL----GSDLPRIKTEIeaLKNLRHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05608    9 LGKGGFGEV-SACQMrATGKLYACKKLNKKRLkkrkGYEGAMVEKRI--LAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYI--ISQDRLSEEETRVVF--RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDyHLQT 167
Cdd:cd05608   86 GDLRYHIynVDEENPGFQEPRACFytAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQT-KTKG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYLGSeADVWSMGILLYVLMCGFLPF----DDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQM 243
Cdd:cd05608  165 YAGTPGFMAPELLLGEEYDYS-VDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSICEAL 243
                        250
                 ....*....|...
gi 375493532 244 LQVDPKKRISMKN 256
Cdd:cd05608  244 LAKDPEKRLGFRD 256
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
11-252 2.98e-20

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: 92.03  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTL----GSDLP---RIKTEIEALKNLrhQHICQLYHVLETANKIF 83
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkqGETLAlneRIMLSLVSTGDC--PFIVCMSYAFHTPDKLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd14223   80 FILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 hlqTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVM---ALYKKIMRGKYDVPKWLSPSSILLL 240
Cdd:cd14223  160 ---ASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTMAVELPDSFSPELRSLL 236
                        250
                 ....*....|..
gi 375493532 241 QQMLQVDPKKRI 252
Cdd:cd14223  237 EGLLQRDVNRRL 248
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
17-152 3.05e-20

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: 87.11  E-value: 3.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDkNTLGSDLPRIKTEIEALK-NLRHQ-HICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGD-DVNNEEGEDLESEMDILRrLKGLElNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532  95 FDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG 152
Cdd:cd13968   80 IAYT-QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-262 3.26e-20

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: 91.29  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEY- 88
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKeIRLEHEEGAPFTAIR-EASLLKDLKHANIVTLHDIIHTKKTLTLVFEYl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 ----------CPGGelfdyiisqdrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKP 157
Cdd:cd07844   81 dtdlkqymddCGGG-----------LSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLArAKS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKDYHLQTCcgSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPF----DDDNVMALYKKIM--------RGK 225
Cdd:cd07844  150 VPSKTYSNEVV--TLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQLHKIFRVLgtpteetwPGV 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 226 YDVPKW---------------------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07844  228 SSNPEFkpysfpfypprplinhaprldRIPHGEELALKFLQYEPKKRISAAEAMKHPY 285
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
15-258 5.08e-20

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: 89.81  E-value: 5.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAcHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd05059   10 KELGSGQFGVVHLG-KWRGKIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRV-VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYhlqTCCGS-- 171
Cdd:cd05059   87 LNYLRERRGKFQTEQLLeMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGL-ARYVLDDEY---TSSVGtk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 172 --LAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVD 247
Cdd:cd05059  163 fpVKWSPPEVFMYSKF-SSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQGyRLYRPHLAPTEVYTIMYSCWHEK 241
                        250
                 ....*....|.
gi 375493532 248 PKKRISMKNLL 258
Cdd:cd05059  242 PEERPTFKILL 252
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
11-260 5.34e-20

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: 90.32  E-value: 5.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIK--IMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHV-LETANK------ 81
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKriRLPNNELARE--KVLREVRALAKLDHPGIVRYFNAwLERPPEgwqekm 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 ----IFMVLEYCPGGELFDYIISQDRLSEEETRV---VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC 154
Cdd:cd14048   86 devyLYIQMQLCRKENLKDWMNRRCTMESRELFVclnIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 155 AK------------PKGNKDYHLQTcCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMcgfLPFDDDNVMALYKKIM 222
Cdd:cd14048  166 TAmdqgepeqtvltPMPAYAKHTGQ-VGTRLYMSPEQIHGNQY-SEKVDIFALGLILFELI---YSFSTQMERIRTLTDV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 375493532 223 RgKYDVPKWLS---PSSILLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd14048  241 R-KLKFPALFTnkyPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
17-260 1.69e-19

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: 88.53  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLpriktEIEALknLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKpSDV-----EIQAC--FRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEyHKLKLIDFGLCAKPKGNKdYHLQTCCGSLAYA 175
Cdd:cd13995   85 EKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS-TKAVLVDFGLSVQMTEDV-YVPKDLRGTEIYM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 176 APELIQGKSYlGSEADVWSMGILLYVLMCGFLPFdddnvmalYKKIMRGKY---------------DVPKWLSPSSILLL 240
Cdd:cd13995  163 SPEVILCRGH-NTKADIYSLGATIIHMQTGSPPW--------VRRYPRSAYpsylyiihkqappleDIAQDCSPAMRELL 233
                        250       260
                 ....*....|....*....|
gi 375493532 241 QQMLQVDPKKRISMKNLLNH 260
Cdd:cd13995  234 EAALERNPNHRSSAAELLKH 253
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
17-213 2.01e-19

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: 88.22  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV-KLACHiltGEmVAIKIMD-KNTLGSDLPRIKTEIEALKNLRHQHICqLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14062    1 IGSGSFGTVyKGRWH---GD-VAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGSSL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRV-VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYHLQTCCGSL 172
Cdd:cd14062   76 YKHLHVLETKFEMLQLIdIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtVKTRWSGSQQFEQPTGSI 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 375493532 173 AYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDN 213
Cdd:cd14062  156 LWMAPEVIrmQDENPYSFQSDVYAFGIVLYELLTGQLPYSHIN 198
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
11-156 2.11e-19

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: 88.28  E-value: 2.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRiktEIEALKNLR-HQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEY---EAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDLL 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493532  90 pgG----ELFDYiiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLIDFGLCAK 156
Cdd:cd14016   79 --GpsleDLFNK--CGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKK 148
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
15-202 2.70e-19

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: 88.53  E-value: 2.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLaCHI-----LTGEMVAIKIMDKNTlGSDLPRIKTEIEALKNLRHQHICQLYHVLETA--NKIFMVLE 87
Cdd:cd14205   10 QQLGKGNFGSVEM-CRYdplqdNTGEVVAVKKLQHST-EEHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd14205   88 YLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKV 167
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 375493532 167 TCCGS--LAYAAPELIQgKSYLGSEADVWSMGILLYVL 202
Cdd:cd14205  168 KEPGEspIFWYAPESLT-ESKFSVASDVWSFGVVLYEL 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
37-267 3.05e-19

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: 87.85  E-value: 3.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  37 VAIKIMDKNTLG-SDLPRiktEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRV-VFR 114
Cdd:cd05068   35 VAVKTLKPGTMDpEDFLR---EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKGRSLQLPQLIdMAA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 115 QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTccGS---LAYAAPELIQGKSYlGSEAD 191
Cdd:cd05068  112 QVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEARE--GAkfpIKWTAPEAANYNRF-SIKSD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 192 VWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGkYDVPKwlsPSSI--LLLQQMLQV---DPKKRISMKNLlnhPWIMQ 265
Cdd:cd05068  189 VWSFGILLTEIVTyGRIPYPGMTNAEVLQQVERG-YRMPC---PPNCppQLYDIMLECwkaDPMERPTFETL---QWKLE 261

                 ..
gi 375493532 266 DY 267
Cdd:cd05068  262 DF 263
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
10-266 3.17e-19

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: 88.94  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKN--TLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06633   23 FVDLHE-IGHGSFGAVYFATNSHTNEVVAIKKMSYSgkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVME 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYhlqt 167
Cdd:cd06633  102 YCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSF---- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 cCGSLAYAAPELI----QGKsYLGsEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGkyDVP-----KWlSPSSIL 238
Cdd:cd06633  178 -VGTPYWMAPEVIlamdEGQ-YDG-KVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQN--DSPtlqsnEW-TDSFRG 251
                        250       260
                 ....*....|....*....|....*...
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd06633  252 FVDYCLQKIPQERPSSAELLRHDFVRRE 279
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
12-257 3.25e-19

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: 87.86  E-value: 3.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHI-LTGEM--VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETaNKIFMVLEY 88
Cdd:cd05056    9 TLGRCIGEGQFGDVYQGVYMsPENEKiaVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITE-NPVWIVMEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQT 167
Cdd:cd05056   88 APLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPF---DDDNVMAlykKIMRG-KYDVPKWLSPSSILLLQQ 242
Cdd:cd05056  168 GKLPIKWMAPESINFRRF-TSASDVWMFGVCMWeILMLGVKPFqgvKNNDVIG---RIENGeRLPMPPNCPPTLYSLMTK 243
                        250
                 ....*....|....*
gi 375493532 243 MLQVDPKKRISMKNL 257
Cdd:cd05056  244 CWAYDPSKRPRFTEL 258
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
15-253 4.35e-19

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: 89.34  E-value: 4.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNT--LGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvlLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY-------HL 165
Cdd:cd05625   87 DMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSkyyqsgdHL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 ----------------------------------QTC-----CGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMCGF 206
Cdd:cd05625  167 rqdsmdfsnewgdpencrcgdrlkplerraarqhQRClahslVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQ 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 207 LPFdddnvmaLYKKIMRGKYDVPKWlspssilllQQMLQVDPKKRIS 253
Cdd:cd05625  246 PPF-------LAQTPLETQMKVINW---------QTSLHIPPQAKLS 276
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
17-251 5.17e-19

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: 86.93  E-value: 5.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHilTGEMVAIKIMDKNTlgsDLPRIKTEIEALKNLRHQHICQLyhVLETANKIFMVLEYCPGGELfD 96
Cdd:cd14068    2 LGDGGFGSVYRAVY--RGEDVAVKIFNKHT---SFRLLRQELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPKGSL-D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEET---RVVFrQIVSAVAYVHSQGYAHRDLKPEN-LLFDEYHKLKLI----DFGL---CAKpkgnkdYHL 165
Cdd:cd14068   74 ALLQQDNASLTRTlqhRIAL-HVADGLRYLHSAMIIYRDLKPHNvLLFTLYPNCAIIakiaDYGIaqyCCR------MGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 166 QTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLY-VLMCGF-----LPFDDD-NVMALYKKIMR--GKYDVPKWlsPSS 236
Cdd:cd14068  147 KTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYdILTCGErivegLKFPNEfDELAIQGKLPDpvKEYGCAPW--PGV 224
                        250
                 ....*....|....*
gi 375493532 237 ILLLQQMLQVDPKKR 251
Cdd:cd14068  225 EALIKDCLKENPQCR 239
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
17-294 5.82e-19

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: 88.68  E-value: 5.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIK---IMDKNTLGSDLprikTEIEALKNLRHQHICQLYHVL--------ETANKIFMV 85
Cdd:cd07854   13 LGCGSNGLVFSAVDSDCDKRVAVKkivLTDPQSVKHAL----REIKIIRRLDHDNIVKVYEVLgpsgsdltEDVGSLTEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDY----IISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD-EYHKLKLIDFGLC--AKPK 158
Cdd:cd07854   89 NSVYIVQEYMETdlanVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLAriVDPH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM---------------- 222
Cdd:cd07854  169 YSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILesvpvvreedrnelln 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 --------------RGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWiMQDYNYPV-EWQSKNPFiHLDD--D 285
Cdd:cd07854  249 vipsfvrndggeprRPLRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPY-MSCYSCPFdEPVSLHPF-HIEDelD 326

                 ....*....
gi 375493532 286 CVTELSVHH 294
Cdd:cd07854  327 DILLMTEIH 335
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
17-213 5.92e-19

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: 86.99  E-value: 5.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV-KLACHiltGEmVAIKIMD-KNTLGSDLPRIKTEIEALKNLRHQHICqLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14150    8 IGTGSFGTVfRGKWH---GD-VAVKILKvTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA-KPKGNKDYHLQTCCGSL 172
Cdd:cd14150   83 YRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATvKTRWSGSQQVEQPSGSI 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 375493532 173 AYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDN 213
Cdd:cd14150  163 LWMAPEVIrmQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNIN 205
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
12-230 6.83e-19

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: 87.02  E-value: 6.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHIlTGEMVAIKIMDKNTLgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05072   10 KLVKKLGAGQFGEVWMGYYN-NSTKVAVKTLKPGTM--SVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQdrlseEETRVVF-------RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYH 164
Cdd:cd05072   87 GSLLDFLKSD-----EGGKVLLpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 165 LQTCCGSLAYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGkYDVPK 230
Cdd:cd05072  162 REGAKFPIKWTAPEAINFGSFT-IKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRG-YRMPR 226
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
7-281 8.89e-19

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: 88.16  E-value: 8.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHV------LETA 79
Cdd:cd07876   19 VLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNqTHAKRAYRELVLLKCVNHKNIISLLNVftpqksLEEF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEycpggeLFDYIISQ---DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd07876   99 QDVYLVME------LMDANLCQvihMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNkdYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM-------------- 222
Cdd:cd07876  173 ACTN--FMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIeqlgtpsaefmnrl 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 ----------RGKYD-------VPKWLSPSSIL-----------LLQQMLQVDPKKRISMKNLLNHPWIMQDYNyPVEWQ 274
Cdd:cd07876  250 qptvrnyvenRPQYPgisfeelFPDWIFPSESErdklktsqardLLSKMLVIDPDKRISVDEALRHPYITVWYD-PAEAE 328

                 ....*..
gi 375493532 275 SKNPFIH 281
Cdd:cd07876  329 APPPQIY 335
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
8-262 9.65e-19

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: 88.04  E-value: 9.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKnTLGSDL--PRIKTEIEALKNLRHQHICQLYHVLETA------ 79
Cdd:cd07879   15 ERYTSLKQ-VGSGAYGSVCSAIDKRTGEKVAIKKLSR-PFQSEIfaKRAYRELTLLKHMQHENVIGLLDVFTSAvsgdef 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYcpggeLFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAkp 157
Cdd:cd07879   93 QDFYLVMPY-----MQTDLqkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 kgNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMR-------------- 223
Cdd:cd07879  166 --HADAEMTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKvtgvpgpefvqkle 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 224 ----GKY--DVPKW-----------LSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07879  244 dkaaKSYikSLPKYprkdfstlfpkASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
17-199 1.05e-18

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: 86.16  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM---DKNTLGSDLprikTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELirfDEETQRTFL----KEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC----------------AK 156
Cdd:cd14221   77 LRGIIKSMDSHYPWSQRVSFaKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpeglrslKK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 375493532 157 PKGNKDYhlqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd14221  157 PDRKKRY---TVVGNPYWMAPEMINGRSY-DEKVDVFSFGIVL 195
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
5-272 1.06e-18

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: 86.83  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELhetiGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd06622    1 DEIEVLDEL----GKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGG---ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLcakpKGN 160
Cdd:cd06622   77 CMEYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGV----SGN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHL-QTCCGSLAYAAPELIQGKSYLGS-----EADVWSMGILLYVLMCGFLPFDD---DNVMALYKKIMRGKY-DVPK 230
Cdd:cd06622  153 LVASLaKTNIGCQSYMAPERIKSGGPNQNptytvQSDVWSLGLSILEMALGRYPYPPetyANIFAQLSAIVDGDPpTLPS 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 375493532 231 WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVE 272
Cdd:cd06622  233 GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVD 274
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
37-258 1.18e-18

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: 86.99  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  37 VAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQ-----------DRL 104
Cdd:cd05101   59 VAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydiNRV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 105 SEEEtrVVFRQIVS-------AVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCCGSL--AYA 175
Cdd:cd05101  139 PEEQ--MTFKDLVSctyqlarGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGL-ARDINNIDYYKKTTNGRLpvKWM 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 176 APELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKKRIS 253
Cdd:cd05101  216 APEALFDRVYT-HQSDVWSFGVLMWeIFTLGGSPYPGIPVEELFKLLKEGhRMDKPANCTNELYMMMRDCWHAVPSQRPT 294

                 ....*
gi 375493532 254 MKNLL 258
Cdd:cd05101  295 FKQLV 299
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-251 1.23e-18

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: 90.29  E-value: 1.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    33 TGEMVAIKIM--DKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA-NKIFMVLEYCPGGELFDYIISQDRLSEEET 109
Cdd:TIGR03903    2 TGHEVAIKLLrtDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   110 RVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKlKLIDFGLCAKPKGNKDYHLQTCC------GSLAYAAPEL 179
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtgVRPHA-KVLDFGIGTLLPGVRDADVATLTrttevlGTPTYCAPEQ 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493532   180 IQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVM-ALYKKIMRGKYDVPKWLSPSSI-LLLQQMLQVDPKKR 251
Cdd:TIGR03903  161 LRGEP-VTPNSDLYAWGLIFLECLTGQRVVQGASVAeILYQQLSPVDVSLPPWIAGHPLgQVLRKALNKDPRQR 233
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
9-285 1.37e-18

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 87.47  E-value: 1.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHeTIGTGGFAKVKLACHILTGEMVAIKIMDK---NTLGSDlpRIKTEIEALKNLRHQHICQLYHV------LETA 79
Cdd:cd07850    1 RYQNLK-PIGSGAQGIVCAAYDTVTGQNVAIKKLSRpfqNVTHAK--RAYRELVLMKLVNHKNIIGLLNVftpqksLEEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEycpggeLFDY----IISQDrLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcA 155
Cdd:cd07850   78 QDVYLVME------LMDAnlcqVIQMD-LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-A 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNkDYHLQTCCGSLAYAAPELIQGKSYlgSE-ADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM------------ 222
Cdd:cd07850  150 RTAGT-SFMMTPYVVTRYYRAPEVILGMGY--KEnVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIeqlgtpsdefms 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 ------------RGKYD-------VPKWLSPSSIL------------LLQQMLQVDPKKRISMKNLLNHPWIMQDYN-YP 270
Cdd:cd07850  227 rlqptvrnyvenRPKYAgysfeelFPDVLFPPDSEehnklkasqardLLSKMLVIDPEKRISVDDALQHPYINVWYDpSE 306
                        330
                 ....*....|....*
gi 375493532 271 VEWQSKNPFIHLDDD 285
Cdd:cd07850  307 VEAPPPAPYDHSIDE 321
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
8-226 1.39e-18

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: 85.85  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIK------IMDKNTLGSDLprikTEIEALKNLRHQHICQLYHVLETANK 81
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqifeMMDAKARQDCV----KEIDLLKQLNHPNVIKYLDSFIEDNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGEL---FDYIISQDRLSEEETR-VVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKP 157
Cdd:cd08228   77 LNIVLELADAGDLsqmIKYFKKQKRLIPERTVwKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL-GRF 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493532 158 KGNKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKY 226
Cdd:cd08228  156 FSSKTTAAHSLVGTPYYMSPERIHENGY-NFKSDIWSLGCLLYEMAALQSPFygDKMNLFSLCQKIEQCDY 225
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
17-199 1.73e-18

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: 85.64  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM---DKNTLGSDLprikTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELirfDEEAQRNFL----KEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC------------------ 154
Cdd:cd14154   77 LKDVLKDMARPLPWAQRVRFaKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmspset 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 155 ----AKPKGNKDYhlqTCCGSLAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd14154  157 lrhlKSPDRKKRY---TVVGNPYWMAPEMLNGRSY-DEKVDIFSFGIVL 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
13-213 1.75e-18

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: 85.88  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKV-KLACHiltGEmVAIKIMDKNT-LGSDLPRIKTEIEALKNLRHQHICqLYHVLETANKIFMVLEYCP 90
Cdd:cd14151   12 VGQRIGSGSFGTVyKGKWH---GD-VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYI-ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA-KPKGNKDYHLQTC 168
Cdd:cd14151   87 GSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQFEQL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 169 CGSLAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDN 213
Cdd:cd14151  167 SGSILWMAPEVIrmQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN 213
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
18-258 1.96e-18

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: 85.01  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  18 GTGGFAKVKLACHILTGEMVAIKimdkntlgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDY 97
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK---------KLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  98 IISQDRLSEEETRVVF--RQIVSAVAYVHSQG---YAHRDLKPENLLFDEYHKLKLIDFGlcAKPKGNKDYHLqTCCGSL 172
Cdd:cd14060   73 LNSNESEEMDMDQIMTwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFG--ASRFHSHTTHM-SLVGTF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd14060  150 PWMAPEVIQSLP-VSETCDTYSYGVVLWEMLTREVPFKGlEGLQVAWLVVEKNeRPTIPSSCPRSFAELMRRCWEADVKE 228

                 ....*...
gi 375493532 251 RISMKNLL 258
Cdd:cd14060  229 RPSFKQII 236
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
8-202 3.35e-18

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: 85.33  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELhetIGTGGFAKVKLaCHI-----LTGEMVAIKIMDKNTLgSDLPRIKTEIEALKNLRHQHICQLYHVLETANK- 81
Cdd:cd05081    6 LKYISQ---LGKGNFGSVEL-CRYdplgdNTGALVAVKQLQHSGP-DQQRDFQREIQILKALHSDFIVKYRGVSYGPGRr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 -IFMVLEYCPGGELFDYII-SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG 159
Cdd:cd05081   81 sLRLVMEYLPSGCLRDFLQrHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 375493532 160 NKDYHLQTCCGS--LAYAAPELIQGKSYlGSEADVWSMGILLYVL 202
Cdd:cd05081  161 DKDYYVVREPGQspIFWYAPESLSDNIF-SRQSDVWSFGVVLYEL 204
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-251 3.81e-18

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: 84.20  E-value: 3.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEmVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCPGGELFD 96
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPE--AFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGSLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAY 174
Cdd:cd14203   79 FLKDGEGKYLKLPQLVdmAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPE-LIQGKSYLGSeaDVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd14203  159 TAPEaALYGRFTIKS--DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESLHELMCQCWRKDPEER 236
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
12-257 4.91e-18

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 84.78  E-value: 4.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHI-----LTGEM-VAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFM 84
Cdd:cd05053   15 TLGKPLGEGAFGQVVKAEAVgldnkPNEVVtVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYI---------ISQDRLSEEETRVVFRQIVS---AVA----YVHSQGYAHRDLKPENLLFDEYHKLKL 148
Cdd:cd05053   95 VVEYASKGNLREFLrarrppgeeASPDDPRVPEEQLTQKDLVSfayQVArgmeYLASKKCIHRDLAARNVLVTEDNVMKI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLcAKPKGNKDYHLQTCCGSLAYA--APELIQGKSYLgSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG- 224
Cdd:cd05053  175 ADFGL-ARDIHHIDYYRKTTNGRLPVKwmAPEALFDRVYT-HQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGh 252
                        250       260       270
                 ....*....|....*....|....*....|...
gi 375493532 225 KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05053  253 RMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
3-260 5.32e-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: 84.31  E-value: 5.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   3 DYDELlkyyELHETIGTGGFAKVKLAChiLTGEMVAIKIMDKN---TLGSDLPRIKTEIEALKNLRHQHICQLYHVLETA 79
Cdd:cd14147    1 SFQEL----RLEEVIGIGGFGKVYRGS--WRGELVAVKAARQDpdeDISVTAESVRQEARLFAMLAHPNIIALKAVCLEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELfDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYA---HRDLKPEN--LLFD------EYHKLKL 148
Cdd:cd14147   75 PNLCLVMEYAAGGPL-SRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNilLLQPienddmEHKTLKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLCakpkgnKDYHLQT---CCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd14147  154 TDFGLA------REWHKTTqmsAAGTYAWMAPEVIKASTF-SKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 375493532 226 YDVPkwlSPSSI-----LLLQQMLQVDPKKRISMKNLLNH 260
Cdd:cd14147  227 LTLP---IPSTCpepfaQLMADCWAQDPHRRPDFASILQQ 263
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
17-259 5.36e-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: 84.48  E-value: 5.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKI-----MDKNTlgsdlpRIKTEIEALKNLR-HQHICQLYHVLETANKI-------F 83
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALKRllsneEEKNK------AIIQEINFMKKLSgHPNIVQFCSAASIGKEEsdqgqaeY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVL-EYCPGG--ELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQG--YAHRDLKPENLLFDEYHKLKLIDFGLCAKPK 158
Cdd:cd14036   82 LLLtELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTCCGSLA-----------YAAPELIQGKSYL--GSEADVWSMGILLYVLMCGFLPFDDDNVMAlykkIMRGK 225
Cdd:cd14036  162 HYPDYSWSAQKRSLVedeitrnttpmYRTPEMIDLYSNYpiGEKQDIWALGCILYLLCFRKHPFEDGAKLR----IINAK 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 375493532 226 YDVPKWLSPSSIL--LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd14036  238 YTIPPNDTQYTVFhdLIRSTLKVNPEERLSITEIVE 273
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
11-263 5.74e-18

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: 84.63  E-value: 5.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPrIKT--EIEALKNLR---HQHICQLYHVLETAN----- 80
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLP-LSTvrEVALLKRLEafdHPNIVRLMDVCATSRtdret 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCpGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpk 158
Cdd:cd07863   81 KVTLVFEHV-DQDLRTYLdkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 gnKDYHLQTCCG----SLAYAAPELIQGKSYlGSEADVWSMGILLY------VLMCG----------F----LPFDDD-- 212
Cdd:cd07863  156 --RIYSCQMALTpvvvTLWYRAPEVLLQSTY-ATPVDMWSVGCIFAemfrrkPLFCGnseadqlgkiFdligLPPEDDwp 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 213 -NVM----ALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07863  233 rDVTlprgAFSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3-271 7.52e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 87.87  E-value: 7.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532    3 DYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNLRHQHICQ-LYHVLETAN 80
Cdd:PTZ00266    7 DGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKErEKSQLVIEVNVMRELKHKNIVRyIDRFLNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   81 -KIFMVLEYCPGGELFDYIISQDRL---SEEETRV-VFRQIVSAVAYVHS-------QGYAHRDLKPENLLFD------- 141
Cdd:PTZ00266   87 qKLYILMEFCDAGDLSRNIQKCYKMfgkIEEHAIVdITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLStgirhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  142 ----EYHKL------KLIDFGLCAKPKGNKDYHlqTCCGSLAYAAPELI--QGKSYlGSEADVWSMGILLYVLMCGFLPF 209
Cdd:PTZ00266  167 kitaQANNLngrpiaKIGDFGLSKNIGIESMAH--SCVGTPYYWSPELLlhETKSY-DDKSDMWALGCIIYELCSGKTPF 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375493532  210 DD-DNVMALYKKIMRGKyDVP-KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPwIMQDYNYPV 271
Cdd:PTZ00266  244 HKaNNFSQLISELKRGP-DLPiKGKSKELNILIKNLLNLSAKERPSALQCLGYQ-IIKNVGPPV 305
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
8-251 1.01e-17

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: 83.93  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHILTGEMVAIK---IMDKNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKkvqIFDLMDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGEL---FDYIISQDRLSEEETR-VVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGN 160
Cdd:cd08229  102 VLELADAGDLsrmIKHFKKQKRLIPEKTVwKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL-GRFFSS 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF--DDDNVMALYKKIMRGKYdvPKWLSPSSIL 238
Cdd:cd08229  181 KTTAAHSLVGTPYYMSPERIHENGY-NFKSDIWSLGCLLYEMAALQSPFygDKMNLYSLCKKIEQCDY--PPLPSDHYSE 257
                        250
                 ....*....|....*..
gi 375493532 239 LLQQMLQV----DPKKR 251
Cdd:cd08229  258 ELRQLVNMcinpDPEKR 274
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
11-261 1.02e-17

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: 83.89  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIK-TEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd07848   83 EKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTEYV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCG--FLPFDD--DNVMALYKKI-------MRGKYDVPKW------- 231
Cdd:cd07848  163 ATRWYRSPELLLGAPY-GKAVDMWSVGCILGELSDGqpLFPGESeiDQLFTIQKVLgplpaeqMKLFYSNPRFhglrfpa 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 232 --------------LSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd07848  242 vnhpqslerrylgiLSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
37-257 1.04e-17

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: 84.25  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  37 VAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYCPGGELFDYI---------ISQDRLSE 106
Cdd:cd05099   47 VAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdYTFDITKV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 107 EETRVVFRQIVSAV-------AYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTCCGSL--AYAAP 177
Cdd:cd05099  127 PEEQLSFKDLVSCAyqvargmEYLESRRCIHRDLAARNVLVTEDNVMKIADFGL-ARGVHDIDYYKKTSNGRLpvKWMAP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 178 ELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKKRISMK 255
Cdd:cd05099  206 EALFDRVYT-HQSDVWSFGILMWeIFTLGGSPYPGIPVEELFKLLREGhRMDKPSNCTHELYMLMRECWHAVPTQRPTFK 284

                 ..
gi 375493532 256 NL 257
Cdd:cd05099  285 QL 286
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
17-200 1.50e-17

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: 82.78  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEM---VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLEtANKIFMVLEYCPGGE 93
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCK-GEPLMLVMELAPLGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGS-- 171
Cdd:cd05060   82 LLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAGRwp 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 375493532 172 LAYAAPELIqgksYLG---SEADVWSMGILLY 200
Cdd:cd05060  162 LKWYAPECI----NYGkfsSKSDVWSYGVTLW 189
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
13-258 1.60e-17

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: 83.92  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGE-------MVAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFM 84
Cdd:cd05100   16 LGKPLGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGEL-----------FDYIISQDRLSEEEtrVVFRQIVS-------AVAYVHSQGYAHRDLKPENLLFDEYHKL 146
Cdd:cd05100   96 LVEYASKGNLreylrarrppgMDYSFDTCKLPEEQ--LTFKDLVScayqvarGMEYLASQKCIHRDLAARNVLVTEDNVM 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 147 KLIDFGLcAKPKGNKDYHLQTCCGSL--AYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMR 223
Cdd:cd05100  174 KIADFGL-ARDVHNIDYYKKTTNGRLpvKWMAPEALFDRVYT-HQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLKE 251
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 375493532 224 G-KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLL 258
Cdd:cd05100  252 GhRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLV 287
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
11-209 1.81e-17

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: 83.59  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMD-KNTLGSDLPRIKtEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd07869    7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRlQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 pGGELFDYIISQ-DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTC 168
Cdd:cd07869   86 -HTDLCQYMDKHpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGL-ARAKSVPSHTYSNE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 375493532 169 CGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd07869  164 VVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
17-258 2.42e-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: 81.96  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDKN---TLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14148    2 IGVGGFGKVYKG--LWRGEEVAVKAARQDpdeDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LfDYIISQDRLSeeeTRVVFR---QIVSAVAYVHSQGYA---HRDLKPENLLFDEYHK--------LKLIDFGLCakpkg 159
Cdd:cd14148   80 L-NRALAGKKVP---PHVLVNwavQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIEnddlsgktLKITDFGLA----- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 nKDYHLQT---CCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPkwlSPSS 236
Cdd:cd14148  151 -REWHKTTkmsAAGTYAWMAPEVIR-LSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLP---IPST 225
                        250       260
                 ....*....|....*....|....*..
gi 375493532 237 -----ILLLQQMLQVDPKKRISMKNLL 258
Cdd:cd14148  226 cpepfARLLEECWDPDPHGRPDFGSIL 252
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
37-251 2.78e-17

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: 81.56  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  37 VAIKIMDKNTLgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQD-RLSEEETRVVFR- 114
Cdd:cd05034   22 VAVKTLKPGTM--SPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRTGEgRALRLPQLIDMAa 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 115 QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTccGS---LAYAAPELIQ-GKSYLGSea 190
Cdd:cd05034  100 QIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGL-ARLIEDDEYTARE--GAkfpIKWTAPEAALyGRFTIKS-- 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 191 DVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGkYDVPKwlsPS--SILLLQQMLQV---DPKKR 251
Cdd:cd05034  175 DVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERG-YRMPK---PPgcPDELYDIMLQCwkkEPEER 237
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
17-212 5.76e-17

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: 81.40  E-value: 5.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIK-IMDKNTLGSDLPRIKTEIEALKNLRH-----QHICQLYHVLETankIFMVLEYCP 90
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKkILIKKVTKRDCMKVLREVKVLAGLQHpnivgYHTAWMEHVQLM---LYIQMQLCE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GgELFDYIISQDRLSEEE--------------TRVVFRQIVSAVAYVHSQGYAHRDLKPENL-LFDEYHKLKLIDFGLCA 155
Cdd:cd14049   91 L-SLWDWIVERNKRPCEEefksapytpvdvdvTTKILQQLLEGVTYIHSMGIVHRDLKPRNIfLHGSDIHVRIGDFGLAC 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 156 K---PKGNKDYHLQ--------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLmcgFLPFDDD 212
Cdd:cd14049  170 PdilQDGNDSTTMSrlnglthtSGVGTCLYAAPEQLEGSHY-DFKSDMYSIGVILLEL---FQPFGTE 233
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
17-258 7.35e-17

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: 80.85  E-value: 7.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDKN---TLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14146    2 IGVGGFGKVYRA--TWKGQEVAVKAARQDpdeDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDrlSEEETRVVFR-----------QIVSAVAYVHSQGYA---HRDLKPENLLFDEY--------HKLKLIDF 151
Cdd:cd14146   80 LNRALAAAN--AAPGPRRARRipphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKiehddicnKTLKITDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 152 GLCakpkgnKDYHLQT---CCGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDV 228
Cdd:cd14146  158 GLA------REWHRTTkmsAAGTYAWMAPEVIK-SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTL 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 229 PkwlSPSSI-----LLLQQMLQVDPKKRISMKNLL 258
Cdd:cd14146  231 P---IPSTCpepfaKLMKECWEQDPHIRPSFALIL 262
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
10-259 9.12e-17

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: 80.76  E-value: 9.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHilTGEMVAIKIMDKNTLGSDLPRIKTEIEALKN--LRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd13980    1 DYLYDKSLGSTRFLKVARARH--DEGLVVVKVFVKPDPALPLRSYKQRLEEIRDrlLELPNVLPFQKVIETDKAAYLIRQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGgELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGlCAKP-------KGN 160
Cdd:cd13980   79 YVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFA-SFKPtylpednPAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAAPELIQGKSY-----------LGSEADVWSMG-ILLYVLMCGFLPFDDDNVMAlYKKimrGKYDV 228
Cdd:cd13980  157 FSYFFDTSRRRTCYIAPERFVDALTldaeserrdgeLTPAMDIFSLGcVIAELFTEGRPLFDLSQLLA-YRK---GEFSP 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 229 PKWLS---PSSIL-LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd13980  233 EQVLEkieDPNIReLILHMIQRDPSKRLSAEDYLK 267
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
12-261 9.64e-17

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: 80.53  E-value: 9.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHE--TIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14051    1 EFHEveKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSvDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQ----DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD---EYHKLKLIDFGLCAKPKGN 160
Cdd:cd14051   81 YCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISrtpNPVSSEEEEEDFEGEEDNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 KDYHLQTCCGSLAYAA----PELIQGKS-YLGSE-----------ADVWSMGILLYVLMCG-FLPFDDDNvmalYKKIMR 223
Cdd:cd14051  161 ESNEVTYKIGDLGHVTsisnPQVEEGDCrFLANEilqenyshlpkADIFALALTVYEAAGGgPLPKNGDE----WHEIRQ 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 375493532 224 GKY-DVPKwLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14051  237 GNLpPLPQ-CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
11-262 1.13e-16

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 81.18  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHI--LTGEMVAIKIMD---KNTLGSDLPRIKtEIEALKNLRHQHICQLYHV-LETANK-IF 83
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKFKgdkEQYTGISQSACR-EIALLRELKHENVVSLVEVfLEHADKsVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPggelFD--YII---SQDRLSEEETRVVFR---QIVSAVAYVHSQGYAHRDLKPENLL----FDEYHKLKLIDF 151
Cdd:cd07842   81 LLFDYAE----HDlwQIIkfhRQAKRVSIPPSMVKSllwQILNGIHYLHSNWVLHRDLKPANILvmgeGPERGVVKIGDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 152 GL---CAKPKgNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVL-------------MCGFLPFDDDNVM 215
Cdd:cd07842  157 GLarlFNAPL-KPLADLDPVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELltlepifkgreakIKKSNPFQRDQLE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 216 AL--------------------YKKIMRGK-------------YDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd07842  236 RIfevlgtptekdwpdikkmpeYDTLKSDTkastypnsllakwMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
34-255 1.17e-16

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 80.13  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  34 GEMVAIKIMDKNTLGSdlPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVF 113
Cdd:cd13992   25 GRTVAIKHITFSRTEK--RTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 114 -RQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC--GSLAYAAPELIQGK--SYLG 187
Cdd:cd13992  103 iKDIVKGMNYLHSSsIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAqhKKLLWTAPELLRGSllEVRG 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 188 S-EADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG--KYDVPKWLSPSS------ILLLQQMLQVDPKKRISMK 255
Cdd:cd13992  183 TqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGgnKPFRPELAVLLDefpprlVLLVKQCWAENPEKRPSFK 259
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
17-258 1.17e-16

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: 79.99  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAcHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd05112   12 IGSGQFGLVHLG-YWLNKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpKGNKDYHLQTCCGS---L 172
Cdd:cd05112   89 YLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMT---RFVLDDQYTSSTGTkfpV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSIL-LLQQMLQVDPKK 250
Cdd:cd05112  166 KWSSPEVFSFSRY-SSKSDVWSFGVLMWeVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYeIMNHCWKERPED 244

                 ....*...
gi 375493532 251 RISMKNLL 258
Cdd:cd05112  245 RPSFSLLL 252
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
110-262 1.44e-16

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: 80.94  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 110 RVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK-LKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELiqgksYLGS 188
Cdd:cd14013  123 KSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGqFKIIDLGAAADLRIGINYIPKEFLLDPRYAPPEQ-----YIMS 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 189 EA--------------------------DVWSMGILLyVLMCgfLPF--DDDNVMALYKKIMRGKYDVPKW-------LS 233
Cdd:cd14013  198 TQtpsappapvaaalspvlwqmnlpdrfDMYSAGVIL-LQMA--FPNlrSDSNLIAFNRQLKQCDYDLNAWrmlveprAS 274
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 375493532 234 PS-----SIL---------LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14013  275 ADlregfEILdlddgagwdLVTKLIRYKPRGRLSASAALAHPY 317
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
15-200 1.73e-16

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: 79.41  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKimdknTLGSDLP---RIK--TEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVK-----TCRETLPpdlKRKflQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQ-DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTC 168
Cdd:cd05041   76 PGGSLLTFLRKKgARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM-SREEEDGEYTVSDG 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 375493532 169 CGSL--AYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:cd05041  155 LKQIpiKWTAPEALNYGRY-TSESDVWSFGILLW 187
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
1-257 3.48e-16

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: 79.24  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   1 MKDYDELLKYyelheTIGTGGFAKVKLA-CHILTGE----MVAIKIMDKNTLGS--DLPRiktEIEALKNLRHQHICQLY 73
Cdd:cd05092    2 IKRRDIVLKW-----ELGEGAFGKVFLAeCHNLLPEqdkmLVAVKALKEATESArqDFQR---EAELLTVLQHQHIVRFY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  74 HVLETANKIFMVLEYCPGGELFDYIISQ---------------DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENL 138
Cdd:cd05092   74 GVCTEGEPLIMVFEYMRHGDLNRFLRSHgpdakildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 139 LFDEYHKLKLIDFGLcAKPKGNKDYHL---QTCCgSLAYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLP-FDDDN 213
Cdd:cd05092  154 LVGQGLVVKIGDFGM-SRDIYSTDYYRvggRTML-PIRWMPPESILYRKFT-TESDIWSFGVVLWeIFTYGKQPwYQLSN 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 375493532 214 VMALyKKIMRGK-YDVPKWLSPSSILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05092  231 TEAI-ECITQGReLERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
13-200 3.62e-16

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: 79.05  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLA-CHILTGE----MVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05049    9 LKRELGEGAFGKVFLGeCYNLEPEqdkmLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQD--------------RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd05049   89 YMEHGDLNKFLRSHGpdaaflasedsapgELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGM 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375493532 154 CAKPKGNKDYHLQtccGS----LAYAAPELIQGKSYLgSEADVWSMGILLY 200
Cdd:cd05049  169 SRDIYSTDYYRVG---GHtmlpIRWMPPESILYRKFT-TESDVWSFGVVLW 215
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
13-258 3.66e-16

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: 79.67  E-value: 3.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHI-LTGEM------VAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFM 84
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAIgLDKDKpnrvtkVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYI----------------ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKL 148
Cdd:cd05098   97 IVEYASKGNLREYLqarrppgmeycynpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKI 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLcAKPKGNKDYHLQTCCGSL--AYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG- 224
Cdd:cd05098  177 ADFGL-ARDIHHIDYYKKTTNGRLpvKWMAPEALFDRIYT-HQSDVWSFGVLLWeIFTLGGSPYPGVPVEELFKLLKEGh 254
                        250       260       270
                 ....*....|....*....|....*....|....
gi 375493532 225 KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLL 258
Cdd:cd05098  255 RMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLV 288
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
10-263 3.83e-16

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: 79.76  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVKLACHILT--GEMVAIK----IMDKNTLgsdLPRIKTEIEALKNLR-HQHICQLYHV-LETANK 81
Cdd:cd07857    1 RYELIKELGQGAYGIVCSARNAETseEETVAIKkitnVFSKKIL---AKRALRELKLLRHFRgHKNITCLYDMdIVFPGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYcpgGELFDY-----IISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL--- 153
Cdd:cd07857   78 FNELYLY---EELMEAdlhqiIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLarg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 CAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCG------------------FLPFDDDNVM 215
Cdd:cd07857  155 FSENPGENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRkpvfkgkdyvdqlnqilqVLGTPDEETL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493532 216 ALYKKIMRGKY-----DVPK----WL----SPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd07857  235 SRIGSPKAQNYirslpNIPKkpfeSIfpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
7-281 4.37e-16

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: 80.13  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHV------LETA 79
Cdd:cd07874   15 VLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNqTHAKRAYRELVLMKCVNHKNIISLLNVftpqksLEEF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCpGGELFDYIisQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG 159
Cdd:cd07874   95 QDVYLVMELM-DANLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKdYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM----------------- 222
Cdd:cd07874  171 TS-FMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIeqlgtpcpefmkklqpt 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 -------RGKY---DVPKwLSPSSIL----------------LLQQMLQVDPKKRISMKNLLNHPWIMQDYNyPVEWQSK 276
Cdd:cd07874  249 vrnyvenRPKYaglTFPK-LFPDSLFpadsehnklkasqardLLSKMLVIDPAKRISVDEALQHPYINVWYD-PAEVEAP 326

                 ....*
gi 375493532 277 NPFIH 281
Cdd:cd07874  327 PPQIY 331
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
17-217 4.70e-16

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: 78.69  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV-KLAchILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd14664    1 IGRGGAGTVyKGV--MPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYI----ISQDRLSEEETRVVFRQIVSAVAYVH---SQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHLQTC 168
Cdd:cd14664   79 ELLhsrpESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGL-AKLMDDKDSHVMSS 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 169 -CGSLAYAAPELIQ-GKSylGSEADVWSMGILLYVLMCGFLPFD----DDNVMAL 217
Cdd:cd14664  158 vAGSYGYIAPEYAYtGKV--SEKSDVYSYGVVLLELITGKRPFDeaflDDGVDIV 210
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
17-221 4.88e-16

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: 78.70  E-value: 4.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDkNTLGSDLPRIK----TEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd14158   23 LGEGGFGVVFKG--YINDKNVAVKKLA-AMVDISTEDLTkqfeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDyiisqdRLS--EEETRVVFRQ---IVSAVA----YVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKD 162
Cdd:cd14158  100 SLLD------RLAclNDTPPLSWHMrckIAQGTAnginYLHENNHIHRDIKSANILLDETFVPKISDFGLArASEKFSQT 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 163 YHLQTCCGSLAYAAPELIQGKsyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKI 221
Cdd:cd14158  174 IMTERIVGTTAYMAPEALRGE--ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDI 230
pknD PRK13184
serine/threonine-protein kinase PknD;
11-253 5.75e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.74  E-value: 5.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgSDLPRIKT----EIEALKNLRHQHICQLYHVLETANKIFMVL 86
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDL--SENPLLKKrflrEAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIIS---QDRLS---EEETRV-----VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA 155
Cdd:PRK13184  82 PYIEGYTLKSLLKSvwqKESLSkelAEKTSVgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNKD-------------YHLQTCCGSLA----YAAPEliqgkSYLGSEA----DVWSMGILLYVLMCGFLPF----- 209
Cdd:PRK13184 162 FKKLEEEdlldidvdernicYSSMTIPGKIVgtpdYMAPE-----RLLGVPAsestDIYALGVILYQMLTLSFPYrrkkg 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 210 ----DDDNV-----MALYKkimrgkyDVPKWLSPssilLLQQMLQVDPKKRIS 253
Cdd:PRK13184 237 rkisYRDVIlspieVAPYR-------EIPPFLSQ----IAMKALAVDPAERYS 278
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
15-200 5.78e-16

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: 78.15  E-value: 5.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLA-------CHIltgeMVAIKIMDKNTLG-----SDLPRiktEIEALKNLRHQHICQLYHVLETaNKI 82
Cdd:cd05040    1 EKLGDGSFGVVRRGewttpsgKVI----QVAVKCLKSDVLSqpnamDDFLK---EVNAMHSLDHPNLIRLYGVVLS-SPL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDyiisqdRLSEEETRV-VFR------QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA 155
Cdd:cd05040   73 MMVTELAPLGSLLD------RLRKDQGHFlISTlcdyavQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 156 KPKGNKDYHLQTCCGSL--AYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:cd05040  147 ALPQNEDHYVMQEHRKVpfAWCAPESLKTRKF-SHASDVWMFGVTLW 192
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
82-251 6.31e-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: 79.14  E-value: 6.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMVLEYCPGGELFDYIISQdRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK---LKLIDFGL---CA 155
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLLSR-RPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLskvCS 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 -------KPKGNKDYHLQTCCGSLAYAAPELIQGksYLGSEADVWSMGILLYVlMCGFLPFDDDNVMA--LYKKIMRGKY 226
Cdd:cd13977  189 gsglnpeEPANVNKHFLSSACGSDFYMAPEVWEG--HYTAKADIFALGIIIWA-MVERITFRDGETKKelLGTYIQQGKE 265
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 375493532 227 DVP--------------------KWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd13977  266 IVPlgeallenpklelqiplkkkKSMNDDMKQLLRDMLAANPQER 310
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
12-199 7.02e-16

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: 78.00  E-value: 7.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHILTgEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCPG 91
Cdd:cd05067   10 KLVERLGAGQFGEVWMGYYNGH-TKVAIKSLKQGSMSPD--AFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYMEN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd05067   86 GSLVDFLKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAK 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd05067  166 FPIKWTAPEAINYGTF-TIKSDVWSFGILL 194
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
20-255 8.22e-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: 77.93  E-value: 8.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  20 GGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYII 99
Cdd:cd14027    4 GGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 100 SQDRLSEEETRVVFrQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC----------- 168
Cdd:cd14027   84 KVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNeqrevdgtakk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 -CGSLAYAAPELIQGKSYLGSE-ADVWSMGILLYVLMCGFLPFDDD-NVMALYKKIMRGKY----DVPKWLSPSSILLLQ 241
Cdd:cd14027  163 nAGTLYYMAPEHLNDVNAKPTEkSDVYSFAIVLWAIFANKEPYENAiNEDQIIMCIKSGNRpdvdDITEYCPREIIDLMK 242
                        250
                 ....*....|....
gi 375493532 242 QMLQVDPKKRISMK 255
Cdd:cd14027  243 LCWEANPEARPTFP 256
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
15-253 8.56e-16

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: 77.28  E-value: 8.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVklachiLTGEM------VAIKIMdKNTLGSDLP-RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05084    2 ERIGRGNFGEV------FSGRLradntpVAVKSC-RETLPPDLKaKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNkdyhLQ 166
Cdd:cd05084   75 LVQGGDFLTFLRTEGpRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDG----VY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCGSL-----AYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSIL-L 239
Cdd:cd05084  151 AATGGMkqipvKWTAPEALNYGRY-SSESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYrL 229
                        250
                 ....*....|....
gi 375493532 240 LQQMLQVDPKKRIS 253
Cdd:cd05084  230 MEQCWEYDPRKRPS 243
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
13-257 9.13e-16

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: 77.46  E-value: 9.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGG 92
Cdd:cd05052   10 MKHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTM--EVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRlsEEETRVVF----RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNkDYHLQTc 168
Cdd:cd05052   88 NLLDYLRECNR--EELNAVVLlymaTQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGD-TYTAHA- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 cGS---LAYAAPEliqGKSY--LGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQ 241
Cdd:cd05052  164 -GAkfpIKWTAPE---SLAYnkFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGyRMERPEGCPPKVYELMR 239
                        250
                 ....*....|....*.
gi 375493532 242 QMLQVDPKKRISMKNL 257
Cdd:cd05052  240 ACWQWNPSDRPSFAEI 255
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
9-251 9.18e-16

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: 77.41  E-value: 9.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHETIGTGGFAKVKLACHILTGE---MVAIKIMDKNTlgSDLPRIK--TEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd05033    4 SYVTIEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSGY--SDKQRLDflTEASIMGQFDHPNVIRLEGVVTKSRPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKD 162
Cdd:cd05033   82 IVTEYMENGSLDKFLRENDgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGL-SRRLEDSE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 YHLQTCCG--SLAYAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDD-DNVMALyKKIMRGkYDVPKWLSPSSIL 238
Cdd:cd05033  161 ATYTTKGGkiPIRWTAPEAIAYRKF-TSASDVWSFGIVMWEVMSyGERPYWDmSNQDVI-KAVEDG-YRLPPPMDCPSAL 237
                        250
                 ....*....|....*
gi 375493532 239 --LLQQMLQVDPKKR 251
Cdd:cd05033  238 yqLMLDCWQKDRNER 252
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
17-200 1.06e-15

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 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: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 77.68  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEM--VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLEtANKIFMVLEYCPGGEL 94
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCE-AEALMLVMEMASGGPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQ-DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGS-- 171
Cdd:cd05115   91 NKFLSGKkDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARSAGKwp 170
                        170       180
                 ....*....|....*....|....*....
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:cd05115  171 LKWYAPECINFRKF-SSRSDVWSYGVTMW 198
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
4-257 1.63e-15

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: 76.78  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   4 YDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDlpriktEIEALKNLRHQHICQLYHVLETANKIF 83
Cdd:cd13991    1 YREEVHWATHQLRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAE------ELMACAGLTSPRVVPLYGAVREGPWVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPEN-LLFDEYHKLKLIDFGL--CAKPKG- 159
Cdd:cd13991   75 IFMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNvLLSSDGSDAFLCDFGHaeCLDPDGl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCC-GSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK---YDVPKWLSPS 235
Cdd:cd13991  155 GKSLFTGDYIpGTETHMAPEVVLGKP-CDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPpplREIPPSCAPL 233
                        250       260
                 ....*....|....*....|..
gi 375493532 236 SILLLQQMLQVDPKKRISMKNL 257
Cdd:cd13991  234 TAQAIQAGLRKEPVHRASAAEL 255
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
56-200 1.70e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 78.73  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  56 TEIEALKNLRHQHICQLYHVLETANKIFMVLEY--CpggELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDL 133
Cdd:PHA03207 135 REIDILKTISHRAIINLIHAYRWKSTVCMVMPKykC---DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDV 211
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375493532 134 KPENLLFDEYHKLKLIDFG----LCAKPKGNKDYHLqtcCGSLAYAAPELIQGKSYLgSEADVWSMGILLY 200
Cdd:PHA03207 212 KTENIFLDEPENAVLGDFGaackLDAHPDTPQCYGW---SGTLETNSPELLALDPYC-AKTDIWSAGLVLF 278
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
12-257 1.78e-15

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: 77.53  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLA-CHILTGEMVAIKI---MDKNTLGSDLPR-IKTEIEALKNL-RHQHICQLYHVLETANKIFMV 85
Cdd:cd05055   38 SFGKTLGAGAFGKVVEAtAYGLSKSDAVMKVavkMLKPTAHSSEREaLMSELKIMSHLgNHENIVNLLGACTIGGPILVI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd05055  118 TEYCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNY 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQtccGS----LAYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMAL-YKKIMRG-KYDVPKWLSPSS 236
Cdd:cd05055  198 VVK---GNarlpVKWMAPESIFNCVYT-FESDVWSYGILLWeIFSLGSNPYPGMPVDSKfYKLIKEGyRMAQPEHAPAEI 273
                        250       260
                 ....*....|....*....|.
gi 375493532 237 ILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05055  274 YDIMKTCWDADPLKRPTFKQI 294
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
12-259 1.78e-15

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily 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: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 77.00  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKV--KLACHILTGEM---VAIKIMDKNTLGSDlpRIKTEIEA--LKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd05032    9 TLIRELGQGSFGMVyeGLAKGVVKGEPetrVAIKTVNENASMRE--RIEFLNEAsvMKEFNCHHVVRLLGVVSTGQPTLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQdRLSEEETRVV--------FR---QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd05032   87 VMELMAKGDLKSYLRSR-RPEAENNPGLgpptlqkfIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 cAKPKGNKDYHLQTCCGSLA--YAAPE-LIQGksYLGSEADVWSMGILLY-VLMCGFLPF---DDDNVMalyKKIMRGKY 226
Cdd:cd05032  166 -TRDIYETDYYRKGGKGLLPvrWMAPEsLKDG--VFTTKSDVWSFGVVLWeMATLAEQPYqglSNEEVL---KFVIDGGH 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 375493532 227 -DVPKWLsPSSILLLQQML-QVDPKKRISMKNLLN 259
Cdd:cd05032  240 lDLPENC-PDKLLELMRMCwQYNPKMRPTFLEIVS 273
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
13-209 1.80e-15

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: 76.99  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKV-KLACHiltGEmVAIKIMD-KNTLGSDLPRIKTEIEALKNLRHQHICqLYHVLETANKIFMVLEYCP 90
Cdd:cd14149   16 LSTRIGSGSFGTVyKGKWH---GD-VAVKILKvVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCA-KPKGNKDYHLQTC 168
Cdd:cd14149   91 GSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQVEQP 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 375493532 169 CGSLAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd14149  171 TGSILWMAPEVIrmQDNNPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
12-230 2.15e-15

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: 76.60  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHILTGEmVAIKIMDKNTLgsDLPRIKTEIEALKNLRHQHICQLyHVLETANKIFMVLEYCPG 91
Cdd:cd05073   14 KLEKKLGAGQFGEVWMATYNKHTK-VAVKTMKPGSM--SVEAFLAEANVMKTLQHDKLVKL-HAVVTKEPIYIITEFMAK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd05073   90 GSLLDFLKSDEGSKQPLPKLIdfSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAK 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375493532 170 GSLAYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGkYDVPK 230
Cdd:cd05073  170 FPIKWTAPEAINFGSFT-IKSDVWSFGILLMeIVTYGRIPYPGMSNPEVIRALERG-YRMPR 229
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
1-211 2.21e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 78.97  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   1 MKDYDELLKYYELHETIGTGGFAKVkLACHI--LTGEMVAIKIMdkNTLGSDLPR------------------IKTEIEA 60
Cdd:PHA03210 140 LKHDDEFLAHFRVIDDLPAGAFGKI-FICALraSTEEAEARRGV--NSTNQGKPKcerliakrvkagsraaiqLENEILA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  61 LKNLRHQHICQLYHVLETANKIFMV---LEYcpggELFDYIIS-----QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRD 132
Cdd:PHA03210 217 LGRLNHENILKIEEILRSEANTYMItqkYDF----DLYSFMYDeafdwKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRD 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 133 LKPENLLFDEYHKLKLIDFGLCA---KPKGNKDYHLqtcCGSLAYAAPELIQGKSYLgSEADVWSMG-ILLYVLMCGFLP 208
Cdd:PHA03210 293 IKLENIFLNCDGKIVLGDFGTAMpfeKEREAFDYGW---VGTVATNSPEILAGDGYC-EITDIWSCGlILLDMLSHDFCP 368

                 ...
gi 375493532 209 FDD 211
Cdd:PHA03210 369 IGD 371
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
17-199 2.45e-15

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: 75.98  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKImdkNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKLkLIDFGLCAKPKGNKDYHLQ-TCCGS 171
Cdd:cd14155   78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdeNGYTAV-VGDFGLAEKIPDYSDGKEKlAVVGS 156
                        170       180
                 ....*....|....*....|....*...
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd14155  157 PYWMAPEVLRGEPY-NEKADVFSYGIIL 183
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
15-251 2.69e-15

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: 75.81  E-value: 2.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAChILTGEMVAIKimdknTLGSDLP-----RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05085    2 ELLGKGNFGEVYKGT-LKDKTPVAVK-----TCKEDLPqelkiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIisQDRLSEEETRVVFRQIVSA---VAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKpkgnKDYHLQ 166
Cdd:cd05085   76 PGGDFLSFL--RKKKDELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ----EDDGVY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCG----SLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLL 240
Cdd:cd05085  150 SSSGlkqiPIKWTAPEALNYGRY-SSESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIM 228
                        250
                 ....*....|.
gi 375493532 241 QQMLQVDPKKR 251
Cdd:cd05085  229 QRCWDYNPENR 239
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
17-224 2.93e-15

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: 76.07  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEM-VAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELF 95
Cdd:cd05113   12 LGTGQFGVVKYG--KWRGQYdVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcakPKGNKDYHLQTCCGS--- 171
Cdd:cd05113   88 NYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL---SRYVLDDEYTSSVGSkfp 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375493532 172 LAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG 224
Cdd:cd05113  165 VRWSPPEVLMYSKF-SSKSDVWAFGVLMWeVYSLGKMPYERFTNSETVEHVSQG 217
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
17-199 3.31e-15

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: 76.14  E-value: 3.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIM---DKNTLGSDLprikTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGE 93
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELircDEETQKTFL----TEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  94 LFDYIISQDRLSEEEtRVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-----AKPKG------NK 161
Cdd:cd14222   77 LKDFLRADDPFPWQQ-KVSFaKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveEKKKPppdkptTK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 375493532 162 DYHLQ--------TCCGSLAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd14222  156 KRTLRkndrkkryTVVGNPYWMAPEMLNGKSY-DEKVDIFSFGIVL 200
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
8-257 4.18e-15

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: 75.29  E-value: 4.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHETIGTGGFAKVKLACHilTGEMVAIKIMDKNTLGSDLpriKTEIEALKNLRHQHICQLYHVLeTANKIFMVLE 87
Cdd:cd05083    5 LQKLTLGEIIGEGEFGAVLQGEY--MGQKVAVKNIKCDVTAQAF---LEETAVMTKLQHKNLVRLLGVI-LHNGLYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKPKGNKDYH 164
Cdd:cd05083   79 LMSKGNLVNFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAkVGSMGVDNSR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 165 LqtccgSLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQ 242
Cdd:cd05083  159 L-----PVKWTAPEALKNKKF-SSKSDVWSYGVLLWeVFSYGRAPYPKMSVKEVKEAVEKGyRMEPPEGCPPDVYSIMTS 232
                        250
                 ....*....|....*
gi 375493532 243 MLQVDPKKRISMKNL 257
Cdd:cd05083  233 CWEAEPGKRPSFKKL 247
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
7-280 4.23e-15

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: 77.01  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG-SDLPRIKTEIEALKNLRHQHICQLYHV------LETA 79
Cdd:cd07875   22 VLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNqTHAKRAYRELVLMKCVNHKNIIGLLNVftpqksLEEF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCpGGELFDYIisQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG 159
Cdd:cd07875  102 QDVYIVMELM-DANLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKdYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIM----------------- 222
Cdd:cd07875  178 TS-FMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIeqlgtpcpefmkklqpt 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 223 -------RGKYD-------VPKWLSPSSIL-----------LLQQMLQVDPKKRISMKNLLNHPWIMQDYNyPVEWQSKN 277
Cdd:cd07875  256 vrtyvenRPKYAgysfeklFPDVLFPADSEhnklkasqardLLSKMLVIDASKRISVDEALQHPYINVWYD-PSEAEAPP 334

                 ...
gi 375493532 278 PFI 280
Cdd:cd07875  335 PKI 337
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
24-262 5.22e-15

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: 75.28  E-value: 5.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  24 KVKLACHILTGEMVAIKIMDKNtlgSDLPRIKTEIealknLRH--QHICQLYHVLETANKIFMVLEYCPGGELFDYIISQ 101
Cdd:cd05576   14 KVLLVMDTRTQETFILKGLRKS---SEYSRERKTI-----IPRcvPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 102 drLSEEETRVVFRQ------------------------IVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKP 157
Cdd:cd05576   86 --LNDKEIHQLFADlderlaaasrfyipeeciqrwaaeMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KgnkdyhlQTCCG---SLAYAAPElIQGKSYLGSEADVWSMGILLYVLMCGflpfdddnvMALYKKIMRG-----KYDVP 229
Cdd:cd05576  164 E-------DSCDSdaiENMYCAPE-VGGISEETEACDWWSLGALLFELLTG---------KALVECHPAGinthtTLNIP 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 230 KWLSPSSILLLQQMLQVDPKKRISM-----KNLLNHPW 262
Cdd:cd05576  227 EWVSEEARSLLQQLLQFNPTERLGAgvagvEDIKSHPF 264
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
12-274 6.02e-15

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: 75.49  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLAchILTGEM-VAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCP 90
Cdd:cd05070   12 QLIKRLGNGQFGEVWMG--TWNGNTkVAIKTLKPGTMSPE--SFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05070   87 KGSLLDFLKDGEGRALKLPNLVdmAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPE-LIQGKSYLGSeaDVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd05070  167 KFPIKWTAPEaALYGRFTIKS--DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPQDCPISLHELMIHCWK 244
                        250       260
                 ....*....|....*....|....*....
gi 375493532 246 VDPKKRISMKNLLNhpwIMQDYNYPVEWQ 274
Cdd:cd05070  245 KDPEERPTFEYLQG---FLEDYFTATEPQ 270
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
15-200 6.68e-15

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 75.49  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEM-----VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05048   11 EELGEGAFGKVYKGELLGPSSEesaisVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIIS----------------QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd05048   91 AHGDLHEFLVRhsphsdvgvssdddgtASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGL 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 cAKPKGNKDYHLQTCCGSLA--YAAPELI-QGKsyLGSEADVWSMGILLY 200
Cdd:cd05048  171 -SRDIYSSDYYRVQSKSLLPvrWMPPEAIlYGK--FTTESDVWSFGVVLW 217
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
13-209 6.68e-15

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: 75.11  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGEmVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCPGG 92
Cdd:cd05071   13 LEVKLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPE--AFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSKG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCG 170
Cdd:cd05071   89 SLLDFLKGEMGKYLRLPQLVdmAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKF 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 375493532 171 SLAYAAPE-LIQGKSYLGSeaDVWSMGILLYVLMC-GFLPF 209
Cdd:cd05071  169 PIKWTAPEaALYGRFTIKS--DVWSFGILLTELTTkGRVPY 207
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
12-224 6.75e-15

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 75.04  E-value: 6.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKlacHILTGEMVAIKIMDKNTLGSD-LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14153    3 EIGELIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEEqLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELfdYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEyHKLKLIDFGLCAKP----KGNKDY 163
Cdd:cd14153   80 GRTL--YSVVRDAkvvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFTISgvlqAGRRED 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 164 HLQTCCGSLAYAAPELI--------QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG 224
Cdd:cd14153  157 KLRIQSGWLCHLAPEIIrqlspeteEDKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSG 225
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
33-262 7.31e-15

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: 75.44  E-value: 7.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  33 TGEMVAIKIMDKNTLGSDLPRIKTEI--------EALKNLRHQHICQLYHVLETANKIFM------------VLEY---- 88
Cdd:cd14011   20 TKQEVSVFVFEKKQLEEYSKRDREQIlellkrgvKQLTRLRHPRILTVQHPLEESRESLAfatepvfaslanVLGErdnm 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 -CPGGELFDYiisqdRLSEEETRVVFRQIVSAVAYVH-SQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQ 166
Cdd:cd14011  100 pSPPPELQDY-----KLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 167 TCCG----------SLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMR--GKYDVPKWLS 233
Cdd:cd14011  175 FREYdpnlpplaqpNLNYLAPEYILSKTC-DPASDMFSLGVLIYaIYNKGKPLFDCVNNLLSYKKNSNqlRQLSLSLLEK 253
                        250       260       270
                 ....*....|....*....|....*....|.
gi 375493532 234 PSSIL--LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14011  254 VPEELrdHVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
9-264 9.50e-15

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: 75.48  E-value: 9.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHeTIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIK------TEIEALKNLRHQHICQLYHVLETANKI 82
Cdd:cd14041    7 RYLLLH-LLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSLDTDS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 F-MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHS--QGYAHRDLKPENLLF---DEYHKLKLIDFGLcAK 156
Cdd:cd14041   86 FcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGL-SK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDYHL-------QTCCGSLAYAAPE-LIQGKS--YLGSEADVWSMGILLYVLMCGFLPFDDDNVMA--LYKKIMRG 224
Cdd:cd14041  165 IMDDDSYNSvdgmeltSQGAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQdiLQENTILK 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 225 KYDV---PK-WLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIM 264
Cdd:cd14041  245 ATEVqfpPKpVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLL 288
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2-263 9.77e-15

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: 75.10  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   2 KDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIE-ALKNLRHQHICQLYHVLETAN 80
Cdd:cd06618    8 KKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDvVLKSHDCPYIVKCYGYFITDS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCpgGELFDYII--SQDRLSEEETRVVFRQIVSAVAYV-HSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKP 157
Cdd:cd06618   88 DVFICMELM--STCLDKLLkrIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKDYHLQTCCGslAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNV-MALYKKIMRGKYDVP---KW 231
Cdd:cd06618  166 VDSKAKTRSAGCA--AYMAPERIdpPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTeFEVLTKILNEEPPSLppnEG 243
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 232 LSPSSILLLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:cd06618  244 FSPDFCSFVDLCLTKDHRYRPKYRELLQHPFI 275
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
13-200 1.48e-14

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: 74.31  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLA-CHILTGE----MVAIKIMdKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05093    9 LKRELGEGAFGKVFLAeCYNLCPEqdkiLVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQD-------------RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLc 154
Cdd:cd05093   88 YMKHGDLNKFLRAHGpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM- 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 375493532 155 AKPKGNKDYHLQTCCGSLA--YAAPELIQGKSYLgSEADVWSMGILLY 200
Cdd:cd05093  167 SRDVYSTDYYRVGGHTMLPirWMPPESIMYRKFT-TESDVWSLGVVLW 213
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
17-259 2.06e-14

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: 73.99  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEM----VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAnKIFMVLEYCPGG 92
Cdd:cd05057   15 LGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSS-QVQLITQLMPLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAK--PKGNKDYHLQTCC 169
Cdd:cd05057   94 CLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGL-AKllDVDEKEYHAEGGK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVD 247
Cdd:cd05057  173 VPIKWMALESIQYRIY-THKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGeRLPQPPICTIDVYMVLVKCWMID 251
                        250
                 ....*....|..
gi 375493532 248 PKKRISMKNLLN 259
Cdd:cd05057  252 AESRPTFKELAN 263
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
17-261 2.07e-14

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: 73.80  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHilTGEMVAIKIMDKNTLGS----------DLPRIKTEIEALKNLRH--------QHICQLYHVLET 78
Cdd:cd14000    2 LGDGGFGSVYRASY--KGEPVAVKIFNKHTSSNfanvpadtmlRHLRATDAMKNFRLLRQeltvlshlHHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLEYCPGGELfDYIISQDRLSEEE-TRVVFR----QIVSAVAYVHSQGYAHRDLKPEN-LLFDEYHK----LKL 148
Cdd:cd14000   80 IHPLMLVLELAPLGSL-DHLLQQDSRSFASlGRTLQQrialQVADGLRYLHSAMIIYRDLKSHNvLVWTLYPNsaiiIKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLCAK--PKGNKDYHlqtccGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKY 226
Cdd:cd14000  159 ADYGISRQccRMGAKGSE-----GTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 375493532 227 DV---PKWLSPSSIL-LLQQMLQVDPKKR---ISMKNLLNHP 261
Cdd:cd14000  234 PPlkqYECAPWPEVEvLMKKCWKENPQQRptaVTVVSILNSP 275
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
2-266 2.11e-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: 74.29  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   2 KDYDELLkYYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETA 79
Cdd:cd06634   10 KDDPEKL-FSDLRE-IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNekWQDIIKEVKFLQKLRHPNTIEYRGCYLRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG 159
Cdd:cd06634   88 HTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYhlqtcCGSLAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPK---WlSP 234
Cdd:cd06634  168 ANSF-----VGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQsghW-SE 241
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 235 SSILLLQQMLQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd06634  242 YFRNFVDSCLQKIPQDRPTSDVLLKHRFLLRE 273
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
9-261 2.23e-14

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: 73.90  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELhETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS-DLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVL 86
Cdd:cd14138    6 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHMLIQN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 EYCPGGELFDYIISQDR----LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---------------DEYHKLK 147
Cdd:cd14138   85 EYCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegdeDEWASNK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 148 LI----DFGLCAKPKGNkdyhlQTCCGSLAYAAPELIQGKSYLGSEADVWSMGiLLYVLMCGFLPFDDDNVMalYKKIMR 223
Cdd:cd14138  165 VIfkigDLGHVTRVSSP-----QVEEGDSRFLANEVLQENYTHLPKADIFALA-LTVVCAAGAEPLPTNGDQ--WHEIRQ 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 375493532 224 GKY-DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14138  237 GKLpRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
9-264 2.29e-14

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: 73.94  E-value: 2.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   9 KYYELHeTIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIK------TEIEALKNLRHQHICQLYHVLETANKI 82
Cdd:cd14040    7 RYLLLH-LLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSLDTDT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 F-MVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHS--QGYAHRDLKPENLLFDE---YHKLKLIDFGLcAK 156
Cdd:cd14040   86 FcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDgtaCGEIKITDFGL-SK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 PKGNKDYHL------QTCCGSLAYAAPE-LIQGKS--YLGSEADVWSMGILLYVLMCGFLPFDDDNVMA------LYKKI 221
Cdd:cd14040  165 IMDDDSYGVdgmdltSQGAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdilqenTILKA 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 375493532 222 MRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIM 264
Cdd:cd14040  245 TEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLL 287
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
12-225 2.98e-14

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: 73.46  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKV-KLACHiltGEmVAIKIMDKNTLGSD-LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd14152    3 ELGELIGQGRWGKVhRGRWH---GE-VAIRLLEIDGNNQDhLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYII-SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEyHKLKLIDFGLCAKP----KGNKDYH 164
Cdd:cd14152   79 KGRTLYSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISgvvqEGRRENE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 165 LQTCCGSLAYAAPELIQ----GKSY----LGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK 225
Cdd:cd14152  158 LKLPHDWLCYLAPEIVRemtpGKDEdclpFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGE 226
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
17-274 3.67e-14

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: 73.18  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEmVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCPGGELFD 96
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPE--AFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGKGSLLD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQD--RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAY 174
Cdd:cd05069   96 FLKEGDgkYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKW 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPE-LIQGKSYLGSeaDVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd05069  176 TAPEaALYGRFTIKS--DVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKLCWKKDPDER 253
                        250       260
                 ....*....|....*....|...
gi 375493532 252 ISMKNLLNhpwIMQDYNYPVEWQ 274
Cdd:cd05069  254 PTFEYIQS---FLEDYFTATEPQ 273
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
15-251 3.93e-14

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: 72.91  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDkNTLGSDLPRIK--TEIEALKNLRHQHICQLYHVLETANKIfmVLEYCPGG 92
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPP-SLHVDDSERMEllEEAKKMEMAKFRHILPVYGICSEPVGL--VMEYMETG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFrQIVSAVAYVHSQG--YAHRDLKPENLLFDEYHKLKLIDFGL--CAKPKGNKDYHLQTC 168
Cdd:cd14025   79 SLEKLLASEPLPWELRFRIIH-ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLakWNGLSHSHDLSRDGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYL-GSEADVWSMGILLYVLMCGFLPF-DDDNVMALYKKIMRGKYD----VPKwLSPSS----IL 238
Cdd:cd14025  158 RGTIAYLPPERFKEKNRCpDTKHDVYSFAIVIWGILTQKKPFaGENNILHIMVKVVKGHRPslspIPR-QRPSEcqqmIC 236
                        250
                 ....*....|...
gi 375493532 239 LLQQMLQVDPKKR 251
Cdd:cd14025  237 LMKRCWDQDPRKR 249
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
15-210 4.13e-14

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 73.52  E-value: 4.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEI--EA--LKNLRHQHICQLYHVLETANkIFMVLEYCP 90
Cdd:cd05108   13 KVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEIldEAyvMASVDNPHVCRLLGICLTST-VQLITQLMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG--NKDYHLQT 167
Cdd:cd05108   92 FGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGL-AKLLGaeEKEYHAEG 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 375493532 168 CCGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMC-GFLPFD 210
Cdd:cd05108  171 GKVPIKWMALESILHRIYT-HQSDVWSYGVTVWELMTfGSKPYD 213
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
57-262 5.87e-14

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: 72.66  E-value: 5.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  57 EIEALKNLR-HQHICQLYHVLeTANKIFMVLEYCPGGELFDYIISQDRLSEEET-------RVVFRQIVSAVAYVHSQGY 128
Cdd:cd14020   53 ERAALEQLQgHRNIVTLYGVF-TNHYSANVPSRCLLLELLDVSVSELLLRSSNQgcsmwmiQHCARDVLEALAFLHHEGY 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 129 AHRDLKPENLLFD-EYHKLKLIDFGLCAKpKGNKDY-HLQTCcgslAYAAPEL----------IQGKSYLGSEADVWSMG 196
Cdd:cd14020  132 VHADLKPRNILWSaEDECFKLIDFGLSFK-EGNQDVkYIQTD----GYRAPEAelqnclaqagLQSETECTSAVDLWSLG 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 197 ILLYVLMCGFLPFD-------DDNVMALYKKIMRGKYDVPKWLsPSSIL--LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14020  207 IVLLEMFSGMKLKHtvrsqewKDNSSAIIDHIFASNAVVNPAI-PAYHLrdLIKSMLHNDPGKRATAEAALCSPF 280
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
17-259 6.52e-14

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: 71.78  E-value: 6.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMdKNTLgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIY-KNDV--DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLK---LIDFGLCAK----PKGNKDYHLqTC 168
Cdd:cd14156   78 LLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREvgemPANDPERKL-SL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMcGFLPFDDDNV---------MALYKKIMRGkydvpkwlSPSSIL- 238
Cdd:cd14156  157 VGSAFWMAPEMLRGEPY-DRKVDVFSFGIVLCEIL-ARIPADPEVLprtgdfgldVQAFKEMVPG--------CPEPFLd 226
                        250       260
                 ....*....|....*....|.
gi 375493532 239 LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd14156  227 LAASCCRMDAFKRPSFAELLD 247
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
17-268 8.56e-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: 72.01  E-value: 8.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRH-QHICQLYHVLETANKIFMVLEycpggeLF 95
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICME------LM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DyiISQDRLSE---EETRVVF-RQIVSAVAY--VHSQGY-------AHRDLKPENLLFDEYHKLKLIDFGLCAkpkgnkd 162
Cdd:cd06616   88 D--ISLDKFYKyvyEVLDSVIpEEILGKIAVatVKALNYlkeelkiIHRDVKPSNILLDRNGNIKLCDFGISG------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 163 yHLQTccgSLA---------YAAPELIQGKSYLGS---EADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRG----- 224
Cdd:cd06616  159 -QLVD---SIAktrdagcrpYMAPERIDPSASRDGydvRSDVWSLGITLYEVATGKFPYPKwNSVFDQLTQVVKGdppil 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 375493532 225 KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPwIMQDYN 268
Cdd:cd06616  235 SNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHP-FIKMYE 277
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
10-266 1.01e-13

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: 72.39  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHEtIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD--LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd06635   27 FSDLRE-IGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNekWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVME 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYhlqt 167
Cdd:cd06635  106 YCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSF---- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 168 cCGSLAYAAPELI--QGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSIL--LLQQM 243
Cdd:cd06635  182 -VGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFrnFVDSC 260
                        250       260
                 ....*....|....*....|...
gi 375493532 244 LQVDPKKRISMKNLLNHPWIMQD 266
Cdd:cd06635  261 LQKIPQDRPTSEELLKHMFVLRE 283
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
11-206 1.49e-13

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: 72.10  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNtLGSDLPRIKTEIEALKNLRHQ-----HICQLYHVLETANKIFMV 85
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL-KN-HPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGgELFDYIiSQDRLSE---EETRVVFRQIVSAVAYVHSQGYAHRDLKPEN-LLFDEY---HKLKLIDFG-LCAKP 157
Cdd:cd14211   79 FEMLEQ-NLYDFL-KQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENiMLVDPVrqpYRVKVIDFGsASHVS 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 375493532 158 KGNKDYHLQtccgSLAYAAPELIQGKSYlgSEA-DVWSMGILLYVLMCGF 206
Cdd:cd14211  157 KAVCSTYLQ----SRYYRAPEIILGLPF--CEAiDMWSLGCVIAELFLGW 200
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
13-257 1.61e-13

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: 71.19  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLA-CHILTGE----MVAIKIMDKNTLGS--DLPRiktEIEALKNLRHQHICQLYHVLETANKIFMV 85
Cdd:cd05094    9 LKRELGEGAFGKVFLAeCYNLSPTkdkmLVAVKTLKDPTLAArkDFQR---EAELLTNLQHDHIVKFYGVCGDGDPLIMV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIIS-----------QDRLSEEETRV-----VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLI 149
Cdd:cd05094   86 FEYMKHGDLNKFLRAhgpdamilvdgQPRQAKGELGLsqmlhIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 150 DFGLcAKPKGNKDYHLQTCCGSLA--YAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKY 226
Cdd:cd05094  166 DFGM-SRDVYSTDYYRVGGHTMLPirWMPPESIMYRKF-TTESDVWSFGVILWeIFTYGKQPWFQLSNTEVIECITQGRV 243
                        250       260       270
                 ....*....|....*....|....*....|..
gi 375493532 227 DVPKWLSPSSIL-LLQQMLQVDPKKRISMKNL 257
Cdd:cd05094  244 LERPRVCPKEVYdIMLGCWQREPQQRLNIKEI 275
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
15-261 1.78e-13

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: 71.11  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSdlpriKTEIEALKNL-------RHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14139    6 EKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGS-----SNEQLALHEVyahavlgHHPHVVRYYSAWAEDDHMIIQNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDRL----SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFdeYHKLKLIDFGLCAKPKGNKDY 163
Cdd:cd14139   81 YCNGGSLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI--CHKMQSSSGVGEEVSNEEDEF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 164 HLQTCC---GSLAYAA----PELIQGKS-YLGSE-----------ADVWSMGiLLYVLMCGFLPFDDDNvmALYKKIMRG 224
Cdd:cd14139  159 LSANVVykiGDLGHVTsinkPQVEEGDSrFLANEilqedyrhlpkADIFALG-LTVALAAGAEPLPTNG--AAWHHIRKG 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 225 KY-DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP 261
Cdd:cd14139  236 NFpDVPQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
17-209 1.97e-13

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 70.64  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV-KLACHiltGEMVAIKIMDKNTLG--SDLPRIKTEIEALKNLRHQHICQLYHV-LETANKIFMVLEYCPGG 92
Cdd:cd14064    1 IGSGSFGKVyKGRCR---NKIVAIKRYRANTYCskSDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQYVSGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDRLSEEETRVVFR-QIVSAVAYVH--SQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd14064   78 SLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQP 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 375493532 170 GSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd14064  158 GNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPF 197
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-234 4.01e-13

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: 70.85  E-value: 4.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   1 MKDYDellkyYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd06649    2 LKDDD-----FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLCAKPkg 159
Cdd:cd06649   77 EISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375493532 160 nKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF---DDDNVMALY-KKIMRGKYDVPKWLSP 234
Cdd:cd06649  155 -IDSMANSFVGTRSYMSPERLQGTHY-SVQSDIWSMGLSLVELAIGRYPIpppDAKELEAIFgRPVVDGEEGEPHSISP 231
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
13-257 4.16e-13

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: 69.99  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKV--KLACHI--LTG-EMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd05045    4 LGKTLGEGEFGKVvkATAFRLkgRAGyTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYI------------------ISQDRLSEEETRVV-----FR-QIVSAVAYVHSQGYAHRDLKPENLLFDEY 143
Cdd:cd05045   84 YAKYGSLRSFLresrkvgpsylgsdgnrnSSYLDNPDERALTMgdlisFAwQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 144 HKLKLIDFGLcAKPKGNKDYHLQTCCGSL--AYAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKK 220
Cdd:cd05045  164 RKMKISDFGL-SRDVYEEDSYVKRSKGRIpvKWMAIESLFDHIYT-TQSDVWSFGVLLWeIVTLGGNPYPGIAPERLFNL 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 221 IMRG-KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05045  242 LKTGyRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
11-200 5.22e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 70.68  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTlgsdlprikTEIEA--LKNLRHQHICQLYHVLETANKIFMVLEY 88
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGT---------TLIEAmlLQNVNHPSVIRMKDTLVSGAITCMVLPH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CpGGELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHlqT 167
Cdd:PHA03209 139 Y-SSDLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFL--G 215
                        170       180       190
                 ....*....|....*....|....*....|...
gi 375493532 168 CCGSLAYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:PHA03209 216 LAGTVETNAPEVLARDKY-NSKADIWSAGIVLF 247
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
15-204 6.59e-13

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: 69.61  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAchILTGEMVAIKIMdkNTLGSDLPRIKTEIEALKNLRHQHICQLYHV----LETANKIFMVLEYCP 90
Cdd:cd14056    1 KTIGKGRYGEVWLG--KYRGEKVAVKIF--SSRDEDSWFRETEIYQTVMLRHENILGFIAAdiksTGSWTQLWLITEYHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYiISQDRLSEEETRVVFRQIVSAVAYVHSQ--GY------AHRDLKPENLLFDEYHKLKLIDFGLC-----AKP 157
Cdd:cd14056   77 HGSLYDY-LQRNTLDTEEALRLAYSAASGLAHLHTEivGTqgkpaiAHRDLKSKNILVKRDGTCCIADLGLAvrydsDTN 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375493532 158 KGNKDYHLQtcCGSLAYAAPELIQGK-------SYlgSEADVWSMGILLYVLMC 204
Cdd:cd14056  156 TIDIPPNPR--VGTKRYMAPEVLDDSinpksfeSF--KMADIYSFGLVLWEIAR 205
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
8-259 6.90e-13

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: 69.42  E-value: 6.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   8 LKYYELHE--TIGTGGF-----AKVKLACHILTGEMVAIKIM---DKNTLGSDLPRiktEIEALKNLRHQHICQLYHVLE 77
Cdd:cd05046    2 FPRSNLQEitTLGRGEFgevflAKAKGIEEEGGETLVLVKALqktKDENLQSEFRR---ELDMFRKLSHKNVVRLLGLCR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  78 TANKIFMVLEYCPGGELFDYI-ISQDR--------LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKL 148
Cdd:cd05046   79 EAEPHYMILEYTDLGDLKQFLrATKSKdeklkpppLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 149 IDFGLCaKPKGNKDY-HLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPF---DDDNVMAlykKIMR 223
Cdd:cd05046  159 SLLSLS-KDVYNSEYyKLRNALIPLRWLAPEAVQEDDF-STKSDVWSFGVLMWeVFTQGELPFyglSDEEVLN---RLQA 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 375493532 224 GKYDVPKWLS-PSSIL-LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd05046  234 GKLELPVPEGcPSRLYkLMTRCWAVNPKDRPSFSELVS 271
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
110-263 6.94e-13

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 71.36  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 110 RVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDE-YHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPEliqgkSYLGS 188
Cdd:PLN03225 258 QTIMRQILFALDGLHSTGIVHRDVKPQNIIFSEgSGSFKIIDLGAAADLRVGINYIPKEFLLDPRYAAPE-----QYIMS 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 189 ----EA----------------------DVWSMGiLLYVLMCgfLPF--DDDNVMALYKKIMRGKYDVPKW---LSPSS- 236
Cdd:PLN03225 333 tqtpSApsapvatalspvlwqlnlpdrfDIYSAG-LIFLQMA--FPNlrSDSNLIQFNRQLKRNDYDLVAWrklVEPRAs 409
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 375493532 237 --------IL---------LLQQMLQVDPKKRISMKNLLNHPWI 263
Cdd:PLN03225 410 pdlrrgfeVLdldggagweLLKSMMRFKGRQRISAKAALAHPYF 453
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-208 8.13e-13

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: 69.70  E-value: 8.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   1 MKDyDELLKYYELhetiGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd06650    2 LKD-DDFEKISEL----GAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPENLLFDEYHKLKLIDFGLCAKPkg 159
Cdd:cd06650   77 EISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 375493532 160 nKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLP 208
Cdd:cd06650  155 -IDSMANSFVGTRSYMSPERLQGTHY-SVQSDIWSMGLSLVEMAVGRYP 201
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
7-259 1.01e-12

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 68.90  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELHE--TIGTGGFAKVKLACHILTGEM----VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05109    3 ILKETELKKvkVLGSGAFGTVYKGIWIPDGENvkipVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 kIFMVLEYCPGGELFDYII-SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPK- 158
Cdd:cd05109   83 -VQLVTQLMPYGCLLDYVReNKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 159 GNKDYHLQTCCGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSS 236
Cdd:cd05109  162 DETEYHADGGKVPIKWMALESILHRRFT-HQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLLEKGeRLPQPPICTIDV 240
                        250       260
                 ....*....|....*....|...
gi 375493532 237 ILLLQQMLQVDPKKRISMKNLLN 259
Cdd:cd05109  241 YMIMVKCWMIDSECRPRFRELVD 263
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
17-266 1.06e-12

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 68.59  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVA-IKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANK----IFMVLEYCPG 91
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESVLKgkkcIVLVTELMTS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQG--YAHRDLKPENLLFD-EYHKLKLIDFGLCAKPKGNkdyHLQTC 168
Cdd:cd14031   98 GTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTS---FAKSV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQgkSYLGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRG--KYDVPKWLSPSSILLLQQMLQ 245
Cdd:cd14031  175 IGTPEFMAPEMYE--EHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSGikPASFNKVTDPEVKEIIEGCIR 252
                        250       260
                 ....*....|....*....|.
gi 375493532 246 VDPKKRISMKNLLNHPWIMQD 266
Cdd:cd14031  253 QNKSERLSIKDLLNHAFFAED 273
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
14-259 1.07e-12

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: 68.46  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  14 HETIGTGGFAKVKLACHILTGE---MVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05063   10 QKVIGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd05063   90 NGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTSG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 170 GSLA--YAAPELIQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGkYDVPKWLS-PSSIL-LLQQML 244
Cdd:cd05063  170 GKIPirWTAPEAIAYRKF-TSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAINDG-FRLPAPMDcPSAVYqLMLQCW 247
                        250
                 ....*....|....*
gi 375493532 245 QVDPKKRISMKNLLN 259
Cdd:cd05063  248 QQDRARRPRFVDIVN 262
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
11-249 1.08e-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: 69.29  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLG---------SDLPRIKTE-------IEALKNLRHQ-HICQLY 73
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL-KNHPSyarqgqievGILARLSNEnadefnfVRAYECFQHRnHTCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  74 HVLETankifmvleycpggELFDYIiSQDRLSEEETRVV---FRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKL 146
Cdd:cd14229   81 EMLEQ--------------NLYDFL-KQNKFSPLPLKVIrpiLQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 147 KLIDFglcakpkGNKDYHLQTCCG----SLAYAAPELIQGKSYlgSEA-DVWSMGILLYVLMCGFlpfdddnvmALYKKI 221
Cdd:cd14229  146 KVIDF-------GSASHVSKTVCStylqSRYYRAPEIILGLPF--CEAiDMWSLGCVIAELFLGW---------PLYPGA 207
                        250       260
                 ....*....|....*....|....*...
gi 375493532 222 MrgKYDVPKWLSPSSILLLQQMLQVDPK 249
Cdd:cd14229  208 L--EYDQIRYISQTQGLPGEQLLNVGTK 233
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
34-200 1.29e-12

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 68.39  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  34 GEMVAIKIMDKNTLgsDLPR-IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELfdyiisQDRLSEEETRV- 111
Cdd:cd14042   30 GNLVAIKKVNKKRI--DLTReVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSL------QDILENEDIKLd 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 112 -VFRQ-----IVSAVAYVH-SQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYhlqtcCGSLAYA------APE 178
Cdd:cd14042  102 wMFRYslihdIVKGMHYLHdSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPP-----DDSHAYYakllwtAPE 176
                        170       180
                 ....*....|....*....|....*
gi 375493532 179 LIQ--GKSYLGS-EADVWSMGILLY 200
Cdd:cd14042  177 LLRdpNPPPPGTqKGDVYSFGIILQ 201
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
15-257 1.62e-12

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: 68.11  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTG----EMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05090   11 EELGECAFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDR------LSEEETRV-----------VFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd05090   91 QGDLHEFLIMRSPhsdvgcSSDEDGTVkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 CAKPKGNKDYHLQT-CCGSLAYAAPELIQ-GKsyLGSEADVWSMGILLYVLMC-GFLP---FDDDNVMALYKKimRGKYD 227
Cdd:cd05090  171 SREIYSSDYYRVQNkSLLPIRWMPPEAIMyGK--FSSDSDIWSFGVVLWEIFSfGLQPyygFSNQEVIEMVRK--RQLLP 246
                        250       260       270
                 ....*....|....*....|....*....|
gi 375493532 228 VPKWLSPSSILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05090  247 CSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
5-262 1.63e-12

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: 68.72  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVkLAC--HILTGEMVAIKIMdKNtLGSDLPRIKTEIEALKNL------------------ 64
Cdd:cd14213    8 DVLRARYEIVDTLGEGAFGKV-VECidHKMGGMHVAVKIV-KN-VDRYREAARSEIQVLEHLnttdpnstfrcvqmlewf 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  65 -RHQHICQLYHVLetankifmvleycpGGELFDYIISQDRL--SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF- 140
Cdd:cd14213   85 dHHGHVCIVFELL--------------GLSTYDFIKENSFLpfPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFv 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 141 --------------DEYH----KLKLIDFGLCAKpkgnKDYHLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVL 202
Cdd:cd14213  151 qsdyvvkynpkmkrDERTlknpDIKVVDFGSATY----DDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEY 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 203 MCGFLPF---DDDNVMALYKKIM------------RGKY---DVPKWLSPSS--------------------------IL 238
Cdd:cd14213  226 YLGFTVFqthDSKEHLAMMERILgplpkhmiqktrKRKYfhhDQLDWDEHSSagryvrrrckplkefmlsqdvdheqlFD 305
                        330       340
                 ....*....|....*....|....
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14213  306 LIQKMLEYDPAKRITLDEALKHPF 329
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
17-200 1.98e-12

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: 67.68  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHIL--TGEMVAIKIMdKNTlgSDLPRIKTEIEALKNLRHQ----HICQLYHVLEtANKIFMVLEYCP 90
Cdd:cd05116    3 LGSGNFGTVKKGYYQMkkVVKTVAVKIL-KNE--ANDPALKDELLREANVMQQldnpYIVRMIGICE-AESWMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCG 170
Cdd:cd05116   79 LGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHG 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 375493532 171 S--LAYAAPELIQGKSYlGSEADVWSMGILLY 200
Cdd:cd05116  159 KwpVKWYAPECMNYYKF-SSKSDVWSFGVLMW 189
UBA_MELK cd14341
UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, ...
281-332 2.81e-12

UBA domain found in maternal embryonic leucine zipper kinase (MELK) and similar proteins; MELK, also called protein kinase Eg3 (pEg3 kinase), protein kinase PK38 (PK38), or tyrosine-protein kinase MELK, is a cell cycle dependent protein kinase involved in diverse cell processes including stem cell renewal, cell cycle progression, cell proliferation, apoptosis and mRNA processing. It is expressed in normal tissues and especially in cancer cells. It is upregulated in cancer tissues and thus may act as potential anticancer target in diverse tumor entities. MELK comprises an N-terminal protein kinase catalytic domain, followed by an ubiquitin-associated (UBA) domain, and a C-terminal autoinhibitory domain of 5'-AMP-activated protein kinase (AMPK).


Pssm-ID: 270526  Cd Length: 52  Bit Score: 61.45  E-value: 2.81e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 281 HLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRL 332
Cdd:cd14341    1 ELDEDCITELSVYYGKSREEMEQLIKEWKYDYLTATYLLLLDKKRRGKPVRL 52
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
17-212 3.20e-12

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: 67.54  E-value: 3.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAchILTGEMVAIKIMDKNtlgSDLP------RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd14159    1 IGEGGFGCVYQA--VMRNTEYAVKRLKED---SELDwsvvknSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYA--HRDLKPENLLFDEYHKLKLIDFGL---CAKPK--GN 160
Cdd:cd14159   76 NGSLEDRLHCQVScpcLSWSQRLHVLLGTARAIQYLHSDSPSliHGDVKSSNILLDAALNPKLGDFGLarfSRRPKqpGM 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 161 KDY--HLQTCCGSLAYAAPELIQ-GKsyLGSEADVWSMGILLYVLMCGFLPFDDD 212
Cdd:cd14159  156 SSTlaRTQTVRGTLAYLPEEYVKtGT--LSVEIDVYSFGVVLLELLTGRRAMEVD 208
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
104-205 5.48e-12

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: 66.36  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 104 LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCaKPKGnkdYHLQTCCGSLAYAAPELIQGK 183
Cdd:cd13975   99 LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC-KPEA---MMSGSIVGTPIHMAPELFSGK 174
                         90       100
                 ....*....|....*....|..
gi 375493532 184 syLGSEADVWSMGILLYVLMCG 205
Cdd:cd13975  175 --YDNSVDVYAFGILFWYLCAG 194
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
17-258 6.95e-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: 66.04  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLAcHILTGEMVAIKIMDKNTLGSDlpRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFD 96
Cdd:cd05114   12 LGSGLFGVVRLG-KWRAQYKVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  97 YIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpKGNKDYHLQTCCGS---L 172
Cdd:cd05114   89 YLRQrRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT---RYVLDDQYTSSSGAkfpV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 173 AYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKWLSPSSILLLQQMLQVDPKK 250
Cdd:cd05114  166 KWSPPEVFNYSKF-SSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRGhRLYRPKLASKSVYEVMYSCWHEKPEG 244

                 ....*...
gi 375493532 251 RISMKNLL 258
Cdd:cd05114  245 RPTFADLL 252
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
12-265 7.29e-12

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: 66.55  E-value: 7.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTG--GFAKVKLACHILTGEMVAIKI-----MDKNtlgsDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFM 84
Cdd:cd08216    1 ELLYEIGKCfkGGGVVHLAKHKPTNTLVAVKKinlesDSKE----DLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYIISQ--DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAK--PKGN 160
Cdd:cd08216   77 VTPLMAYGSCRDLLKTHfpEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSmvKHGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 161 K----DYHLQTCCGSLAYAAPELIQgKSYLG--SEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG---------- 224
Cdd:cd08216  157 RqrvvHDFPKSSEKNLPWLSPEVLQ-QNLLGynEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGttpqlldcst 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 225 -----------------------KYDVP--KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQ 265
Cdd:cd08216  236 ypleedsmsqsedsstehpnnrdTRDIPyqRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQ 301
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
10-263 7.94e-12

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: 66.48  E-value: 7.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  10 YYELHETIGTGGFAKVkLACHILT--GEMVAIKIMDKNtlgsDLPRI--KTEIEALKNLR------HQHICQLYHVLETA 79
Cdd:cd14135    1 RYRVYGYLGKGVFSNV-VRARDLArgNQEVAIKIIRNN----ELMHKagLKELEILKKLNdadpddKKHCIRLLRHFEHK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  80 NKIFMVLEyCPGGELFDYIISQDR---LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHK-LKLIDFGlCA 155
Cdd:cd14135   76 NHLCLVFE-SLSMNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFG-SA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 KPKGNKDY--HLQtccgSLAYAAPELIQGKSYlGSEADVWSMGILLYVL------------------------------- 202
Cdd:cd14135  154 SDIGENEItpYLV----SRFYRAPEIILGLPY-DYPIDMWSVGCTLYELytgkilfpgktnnhmlklmmdlkgkfpkkml 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 203 ------------MCGFLPFDDDNVMA-LYKKIMR---GKYDVPKWLSPSSIL-------------LLQQMLQVDPKKRIS 253
Cdd:cd14135  229 rkgqfkdqhfdeNLNFIYREVDKVTKkEVRRVMSdikPTKDLKTLLIGKQRLpdedrkkllqlkdLLDKCLMLDPEKRIT 308
                        330
                 ....*....|
gi 375493532 254 MKNLLNHPWI 263
Cdd:cd14135  309 PNEALQHPFI 318
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
35-225 8.56e-12

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: 65.94  E-value: 8.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  35 EMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHV-LETANKIFMVLEYCPGGELFDYIiSQDRLSEEETRVVF 113
Cdd:cd05043   35 EEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVcIEDGEKPMVLYPYMNWGNLKLFL-QQCRLSEANNPQAL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 114 R---------QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKGNKDYHlqtCCGS-----LAYAAPEL 179
Cdd:cd05043  114 StqqlvhmalQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNAL-SRDLFPMDYH---CLGDnenrpIKWMSLES 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 180 IQGKSYlGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRGK 225
Cdd:cd05043  190 LVNKEY-SSASDVWSFGVLLWELMTlGQTPYVEIDPFEMAAYLKDGY 235
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
11-263 9.46e-12

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: 66.45  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKI-----------MDkntlgsdlpriktEIEALK--------NLRHQHICQ 71
Cdd:cd14136   12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVvksaqhyteaaLD-------------EIKLLKcvreadpkDPGREHVVQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  72 LY----HVLETANKIFMVLEYCpGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQ-GYAHRDLKPEN-LLFDEY 143
Cdd:cd14136   79 LLddfkHTGPNGTHVCMVFEVL-GPNLLKLIKRYNYrgIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENvLLCISK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 144 HKLKLIDFglcakpkGNK---DYH----LQTccgsLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFD------ 210
Cdd:cd14136  158 IEVKIADL-------GNAcwtDKHftedIQT----RQYRSPEVILGAGY-GTPADIWSTACMAFELATGDYLFDphsged 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 211 ---DDNVMALY---------------------------------------KKIMRGKYDVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd14136  226 ysrDEDHLALIiellgriprsiilsgkysreffnrkgelrhisklkpwplEDVLVEKYKWSKEEAKEFASFLLPMLEYDP 305
                        330
                 ....*....|....*
gi 375493532 249 KKRISMKNLLNHPWI 263
Cdd:cd14136  306 EKRATAAQCLQHPWL 320
KA1 pfam02149
Kinase associated domain 1;
567-610 1.38e-11

Kinase associated domain 1;


Pssm-ID: 426623  Cd Length: 44  Bit Score: 59.41  E-value: 1.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 375493532  567 TMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV 610
Cdd:pfam02149   1 VVKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSELRL 44
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
13-260 1.72e-11

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 65.20  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTG-----EMVAIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVL 86
Cdd:cd05054   11 LGKPLGRGAFGKVIQASAFGIDksatcRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGGPLMVI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  87 -EYCPGGELFDYI--------------------------ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLL 139
Cdd:cd05054   91 vEFCKFGNLSNYLrskreefvpyrdkgardveeeedddeLYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNIL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 140 FDEYHKLKLIDFGLCAKPKGNKDYHLQTCCG-SLAYAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPF-----DDD 212
Cdd:cd05054  171 LSENNVVKICDFGLARDIYKDPDYVRKGDARlPLKWMAPESIFDKVY-TTQSDVWSFGVLLWeIFSLGASPYpgvqmDEE 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 213 nvmaLYKKIMRG-KYDVPKWLSPSsilLLQQMLQV---DPKKRISMKNLLNH 260
Cdd:cd05054  250 ----FCRRLKEGtRMRAPEYTTPE---IYQIMLDCwhgEPKERPTFSELVEK 294
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
11-199 2.13e-11

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: 65.05  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTG-EMVAIKIMDKNTLGSDLP----RIKTEIEALKNLRHQHICQLYHVLETA-----N 80
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDLKNGgRFVALKRVRVQTGEEGMPlstiREVAVLRHLETFEHPNVVRLFDVCTVSrtdreT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 KIFMVLEYCpGGELFDYI--ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCakpk 158
Cdd:cd07862   83 KLTLVFEHV-DQDLTTYLdkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA---- 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 375493532 159 gnKDYHLQTCCGS----LAYAAPELIQGKSYlGSEADVWSMGILL 199
Cdd:cd07862  158 --RIYSFQMALTSvvvtLWYRAPEVLLQSSY-ATPVDLWSVGCIF 199
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
56-260 2.56e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.79  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  56 TEIEALKNLRHQHICQLYHVLeTANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKP 135
Cdd:PHA03212 132 TEAHILRAINHPSIIQLKGTF-TYNKFTCLILPRYKTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKA 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 136 ENLLFDEYHKLKLIDFGLCAKP---KGNKDYHLqtcCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGF------ 206
Cdd:PHA03212 211 ENIFINHPGDVCLGDFGAACFPvdiNANKYYGW---AGTIATNAPELLARDPY-GPAVDIWSAGIVLFEMATCHdslfek 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 207 --------------------------LPFD-----DDNVMALYKKIMRGKYDVPKWLSPSSI-----LLLQQMLQVDPKK 250
Cdd:PHA03212 287 dgldgdcdsdrqikliirrsgthpneFPIDaqanlDEIYIGLAKKSSRKPGSRPLWTNLYELpidleYLICKMLAFDAHH 366
                        250
                 ....*....|
gi 375493532 251 RISMKNLLNH 260
Cdd:PHA03212 367 RPSAEALLDF 376
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
15-258 2.61e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 64.29  E-value: 2.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLACHILTGEMV--AIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEYCPG 91
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  92 GELFDY-----IISQD-----------RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLca 155
Cdd:cd05047   81 GNLLDFlrksrVLETDpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 156 kPKGNKDYHLQTcCGSLA--YAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYDVPKW 231
Cdd:cd05047  159 -SRGQEVYVKKT-MGRLPvrWMAIESLNYSVYT-TNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEKLPQGyRLEKPLN 235
                        250       260
                 ....*....|....*....|....*..
gi 375493532 232 LSPSSILLLQQMLQVDPKKRISMKNLL 258
Cdd:cd05047  236 CDDEVYDLMRQCWREKPYERPSFAQIL 262
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
31-199 2.93e-11

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 64.11  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  31 ILTGEMVAIKIMDKNTLGSDlPRIKTEIEALKNLRHQHICQLYH-VLETANkIFMVLEYCPGGELFDYIISQDRLSEEET 109
Cdd:cd14045   27 IYDGRTVAIKKIAKKSFTLS-KRIRKEVKQVRELDHPNLCKFIGgCIEVPN-VAIITEYCPKGSLNDVLLNEDIPLNWGF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 110 RVVF-RQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSL--AYAAPELIQGKSYL 186
Cdd:cd14045  105 RFSFaTDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGYQQRLmqVYLPPENHSNTDTE 184
                        170
                 ....*....|....
gi 375493532 187 GSEA-DVWSMGILL 199
Cdd:cd14045  185 PTQAtDVYSYAIIL 198
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
13-251 3.10e-11

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: 64.17  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGE---MVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05064    9 IERILGTGRFGELCRGCLKLPSKrelPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05064   89 SNGALDSFLRKHEgQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEAIYTTMSG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 169 CGSLAYAAPELIQgKSYLGSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVPKWLSPssiLLLQQML-- 244
Cdd:cd05064  169 KSPVLWAAPEAIQ-YHHFSSASDVWSFGIVMWEVMSyGERPYWDMSGQDVIKAVEDGfRLPAPRNCPN---LLHQLMLdc 244

                 ....*...
gi 375493532 245 -QVDPKKR 251
Cdd:cd05064  245 wQKERGER 252
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
11-257 3.28e-11

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 64.17  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHIL---TGEMVAIKIMDKNTL-GSDLPRIKTEIEALKNLRHQHICQLYHV-LETANK---- 81
Cdd:cd05074   11 FTLGRMLGKGEFGSVREAQLKSedgSFQKVAVKMLKADIFsSSDIEEFLREAACMKEFDHPNVIKLIGVsLRSRAKgrlp 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  82 IFMV-LEYCPGGELFDYIISQdRLSEE------ETRVVFR-QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL 153
Cdd:cd05074   91 IPMViLPFMKHGDLHTFLLMS-RIGEEpftlplQTLVRFMiDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 154 cAKPKGNKDYHLQTCCGSL--AYAAPELIQGKSYLgSEADVWSMGILLYVLMC-GFLPFDDDNVMALYKKIMRG-KYDVP 229
Cdd:cd05074  170 -SKKIYSGDYYRQGCASKLpvKWLALESLADNVYT-THSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKGnRLKQP 247
                        250       260
                 ....*....|....*....|....*...
gi 375493532 230 KWLSPSSILLLQQMLQVDPKKRISMKNL 257
Cdd:cd05074  248 PDCLEDVYELMCQCWSPEPKCRPSFQHL 275
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
17-259 3.32e-11

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: 63.98  E-value: 3.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV--KLACHIL---TGEM-VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCP 90
Cdd:cd05044    3 LGSGAFGEVfeGTAKDILgdgSGETkVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  91 GGELFDYI-------ISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDE--YHK--LKLIDFGLcAKPKG 159
Cdd:cd05044   83 GGDLLSYLraarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSkdYRErvVKIGDFGL-ARDIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCCGSLA--YAAPE-LIQGksYLGSEADVWSMGILLY-VLMCGFLPFDD-DNVMALYKKIMRGKYDVPKwLSP 234
Cdd:cd05044  162 KNDYYRKEGEGLLPvrWMAPEsLVDG--VFTTQSDVWAFGVLMWeILTLGQQPYPArNNLEVLHFVRAGGRLDQPD-NCP 238
                        250       260
                 ....*....|....*....|....*.
gi 375493532 235 SSIL-LLQQMLQVDPKKRISMKNLLN 259
Cdd:cd05044  239 DDLYeLMLRCWSTDPEERPSFARILE 264
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
11-209 3.92e-11

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: 63.92  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDkntlgSDLPR--IKTEIEALKNLRHQ-HICQLYHVLETANKIFMVLE 87
Cdd:cd14129    2 WKVLRKIGGGGFGEIYDALDLLTRENVALKVES-----AQQPKqvLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YcPGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEY----HKLKLIDFGLCAK----- 156
Cdd:cd14129   77 L-QGRNLADLRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFpstcRKCYMLDFGLARQftnsc 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375493532 157 -----PKGNKDYHlqtccGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd14129  156 gdvrpPRAVAGFR-----GTVRYASINAHRNRE-MGRHDDLWSLFYMLVEFVVGQLPW 207
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
15-200 5.08e-11

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: 64.00  E-value: 5.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAChiLTGEMVAIKIM---DKNTLGSDlprikTEIEALKNLRHQHICQLYHVLETAN----KIFMVLE 87
Cdd:cd13998    1 EVIGKGRFGEVWKAS--LKNEPVAVKIFssrDKQSWFRE-----KEIYRTPMLKHENILQFIAADERDTalrtELWLVTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQ---------GYAHRDLKPENLLFDEYHKLKLIDFGLC---- 154
Cdd:cd13998   74 FHPNGSL*DYL-SLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAvrls 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375493532 155 -AKPKGNKDYHLQTccGSLAYAAPELIQG-------KSYLgsEADVWSMGILLY 200
Cdd:cd13998  153 pSTGEEDNANNGQV--GTKRYMAPEVLEGainlrdfESFK--RVDIYAMGLVLW 202
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
11-299 5.19e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 64.34  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG--------SDLPRIKTE-------IEALKNLRHQ-HICQLYH 74
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYarqgqievSILARLSTEsaddynfVRAYECFQHKnHTCLVFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  75 VLETankifmvleycpggELFDYIiSQDRLSE---EETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKLK 147
Cdd:cd14227   97 MLEQ--------------NLYDFL-KQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 148 LIDFGLCAK-PKGNKDYHLQtccgSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMCGFlpfdddnvmALYKKImrGKY 226
Cdd:cd14227  162 VIDFGSASHvSKAVCSTYLQ----SRYYRAPEIILGLPFC-EAIDMWSLGCVIAELFLGW---------PLYPGA--SEY 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493532 227 DVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPwimqdynYPVeWQSKNPfihldDDCVTELSVHHRNNRQ 299
Cdd:cd14227  226 DQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSP-------YPL-WRLKTP-----EDHEAETGIKSKEARK 285
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
15-221 5.54e-11

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: 63.89  E-value: 5.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAchILTGEMVAIKIM---DKNTLGSDLpriktEIEALKNLRHQHICQLY----HVLETANKIFMVLE 87
Cdd:cd14053    1 EIKARGRFGAVWKA--QYLNRLVAVKIFplqEKQSWLTER-----EIYSLPGMKHENILQFIgaekHGESLEAEYWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGGELFDYIISQDrLSEEETRVVFRQIVSAVAYVHS------QGY----AHRDLKPENLLFDEYHKLKLIDFGLCAKP 157
Cdd:cd14053   74 FHERGSLCDYLKGNV-ISWNELCKIAESMARGLAYLHEdipatnGGHkpsiAHRDFKSKNVLLKSDLTACIADFGLALKF 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493532 158 KGNK---DYHLQTccGSLAYAAPELIQGKSYLGSEA----DVWSMGILLYVLM--CGFLPFDDDNVMALYKKI 221
Cdd:cd14053  153 EPGKscgDTHGQV--GTRRYMAPEVLEGAINFTRDAflriDMYAMGLVLWELLsrCSVHDGPVDEYQLPFEEE 223
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
11-206 9.14e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 63.57  E-value: 9.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEAL---KNLRHQHICQLYHVLETANKIFMVLE 87
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRlssENADEYNFVRSYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  88 YCPGgELFDYIiSQDRLSE---EETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF----DEYHKLKLIDFGLCAK-PKG 159
Cdd:cd14228   97 MLEQ-NLYDFL-KQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHvSKA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 375493532 160 NKDYHLQtccgSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMCGF 206
Cdd:cd14228  175 VCSTYLQ----SRYYRAPEIILGLPFC-EAIDMWSLGCVIAELFLGW 216
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
12-251 9.25e-11

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 63.48  E-value: 9.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHI-----LTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHqHIcQLYHVLETANK----I 82
Cdd:cd14207   10 KLGKSLGRGAFGKVVQASAFgikksPTCRVVAVKMLKEGATASEYKALMTELKILIHIGH-HL-NVVNLLGACTKsggpL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 FMVLEYCPGGELFDYIISQ------------------------------------------------------DRLSEEE 108
Cdd:cd14207   88 MVIVEYCKYGNLSNYLKSKrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedkslsDVEEEEE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 109 TRVVFR--------------QIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCG-SLA 173
Cdd:cd14207  168 DSGDFYkrpltmedlisysfQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDARlPLK 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 174 YAAPELIQGKSYlGSEADVWSMGILLY-VLMCGFLPFD----DDNVMALYKKIMRGKydVPKWLSPSSILLLQQMLQVDP 248
Cdd:cd14207  248 WMAPESIFDKIY-STKSDVWSYGVLLWeIFSLGASPYPgvqiDEDFCSKLKEGIRMR--APEFATSEIYQIMLDCWQGDP 324

                 ...
gi 375493532 249 KKR 251
Cdd:cd14207  325 NER 327
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-264 1.26e-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: 62.84  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  18 GTGGFakVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDY 97
Cdd:cd06615   12 GNGGV--VTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  98 IISQDRLSEEETRVVFRQIVSAVAY---VHSqgYAHRDLKPENLLFDEYHKLKLIDFGLCAKPkgnKDYHLQTCCGSLAY 174
Cdd:cd06615   90 LKKAGRIPENILGKISIAVLRGLTYlreKHK--IMHRDVKPSNILVNSRGEIKLCDFGVSGQL---IDSMANSFVGTRSY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 175 AAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF-------------DDDNVMALYKKIMRGKYDVP------------ 229
Cdd:cd06615  165 MSPERLQGTHY-TVQSDIWSLGLSLVEMAIGRYPIpppdakeleamfgRPVSEGEAKESHRPVSGHPPdsprpmaifell 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 375493532 230 -------------KWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIM 264
Cdd:cd06615  244 dyivnepppklpsGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
11-203 1.92e-10

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: 61.75  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNT------LGSDLPRIKTEIEALKNLRHQHICQLYHVLetankiFM 84
Cdd:cd14128    2 YRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKArhpqllYESKLYKILQGGVGIPHIRWYGQEKDYNVL------VM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  85 VLEYCPGGELFDYiiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFD---EYHKLKLIDFGLCAKPKGNK 161
Cdd:cd14128   76 DLLGPSLEDLFNF--CSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGigrHCNKLFLIDFGLAKKYRDSR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375493532 162 D-YHLQ-----TCCGSLAYAAPeliqgKSYLGSEA----DVWSMGillYVLM 203
Cdd:cd14128  154 TrQHIPyredkNLTGTARYASI-----NAHLGIEQsrrdDMESLG---YVLM 197
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
17-221 2.15e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTlgsDLPRIKTEIEALKNLR-HQHICQLYHVLETANKIFMVLEYCpGGELF 95
Cdd:cd14017    8 IGGGGFGEIYKVRDVVDGEEVAMKVESKSQ---PKQVLKMEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMTLL-GPNLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  96 DYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPEN----LLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCC 169
Cdd:cd14017   84 ELRRSQPRgkFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNfaigRGPSDERTVYILDFGLARQYTNKDGEVERPPR 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375493532 170 ------GSLAYAAPELIQGKSyLGSEADVWSmgiLLYVL---MCGFLPF----DDDNVMALYKKI 221
Cdd:cd14017  164 naagfrGTVRYASVNAHRNKE-QGRRDDLWS---WFYMLiefVTGQLPWrklkDKEEVGKMKEKI 224
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
5-262 2.15e-10

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: 62.34  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVkLAC--HILTGEMVAIKIMDKNTLGSDLPRIktEIEAL-----KNLRHQHIC-QLYHVL 76
Cdd:cd14215    8 DWLQERYEIVSTLGEGTFGRV-VQCidHRRGGARVALKIIKNVEKYKEAARL--EINVLekineKDPENKNLCvQMFDWF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  77 ETANKIFMVLEYCpGGELFDYIISQDRL--SEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF-------------- 140
Cdd:cd14215   85 DYHGHMCISFELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekk 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 141 -DEY----HKLKLIDFGlcakpKGNKDY-HLQTCCGSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPF---DD 211
Cdd:cd14215  164 rDERsvksTAIRVVDFG-----SATFDHeHHSTIVSTRHYRAPEVILELGW-SQPCDVWSIGCIIFEYYVGFTLFqthDN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 212 DNVMALYKKIM------------------RGKYDvpkWLSPSS--------------------------ILLLQQMLQVD 247
Cdd:cd14215  238 REHLAMMERILgpipsrmirktrkqkyfyHGRLD---WDENTSagryvrenckplrryltseaeehhqlFDLIESMLEYE 314
                        330
                 ....*....|....*
gi 375493532 248 PKKRISMKNLLNHPW 262
Cdd:cd14215  315 PSKRLTLAAALKHPF 329
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
7-210 2.18e-10

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 62.01  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELH--ETIGTGGFAKVKLACHILTGEMV----AIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05110    3 ILKETELKrvKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 kIFMVLEYCPGGELFDYIIS-QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKG 159
Cdd:cd05110   83 -IQLVTQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEG 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375493532 160 N-KDYHLQTCCGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLMC-GFLPFD 210
Cdd:cd05110  162 DeKEYNADGGKMPIKWMALECIHYRKFT-HQSDVWSYGVTIWELMTfGGKPYD 213
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
93-200 2.45e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 62.99  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  93 ELFDYIISQDR-LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKD----YHLqt 167
Cdd:PHA03211 245 DLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARGSWStpfhYGI-- 322
                         90       100       110
                 ....*....|....*....|....*....|...
gi 375493532 168 cCGSLAYAAPELIQGKSYLGSeADVWSMGILLY 200
Cdd:PHA03211 323 -AGTVDTNAPEVLAGDPYTPS-VDIWSAGLVIF 353
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
11-156 2.72e-10

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: 61.61  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKimdkntlgsdLPRIKTeiealknlRHQHI---CQLYHVLETANKI----- 82
Cdd:cd14125    2 YRLGRKIGSGSFGDIYLGTNIQTGEEVAIK----------LESVKT--------KHPQLlyeSKLYKILQGGVGIpnvrw 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  83 --------FMVLEYC-PGGE-LFDYiiSQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLF---DEYHKLKLI 149
Cdd:cd14125   64 ygvegdynVMVMDLLgPSLEdLFNF--CSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMglgKKGNLVYII 141

                 ....*..
gi 375493532 150 DFGLCAK 156
Cdd:cd14125  142 DFGLAKK 148
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
17-262 2.83e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPR--IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGEL 94
Cdd:cd14026    5 LSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERncLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  95 FDYIISQDRLSEEETRVVFR---QIVSAVAYVH--SQGYAHRDLKPENLLFD-EYHkLKLIDFGLC-------AKPKGNK 161
Cdd:cd14026   85 NELLHEKDIYPDVAWPLRLRilyEIALGVNYLHnmSPPLLHHDLKTQNILLDgEFH-VKIADFGLSkwrqlsiSQSRSSK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 162 DYHLQtccGSLAYAAPELIQ--GKSYLGSEADVWSMGILLYVLMCGFLPFDD-DNVMALYKKIMRGKYDVpkwlspssil 238
Cdd:cd14026  164 SAPEG---GTIIYMPPEEYEpsQKRRASVKHDIYSYAIIMWEVLSRKIPFEEvTNPLQIMYSVSQGHRPD---------- 230
                        250       260
                 ....*....|....*....|....
gi 375493532 239 LLQQMLQVDPKKRISMKNLLNHPW 262
Cdd:cd14026  231 TGEDSLPVDIPHRATLINLIESGW 254
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
17-259 3.03e-10

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 61.52  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  17 IGTGGFAKV--KLACHILTGEM---VAIKIMdkNTLGSDLPRIK--TEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05061   14 LGQGSFGMVyeGNARDIIKGEAetrVAVKTV--NESASLRERIEflNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQDRLSE----------EETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLcAKPKG 159
Cdd:cd05061   92 AHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGM-TRDIY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 160 NKDYHLQTCCGSL--AYAAPELIQGKSYLGSeADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRGKY-DVPKWLSPS 235
Cdd:cd05061  171 ETDYYRKGGKGLLpvRWMAPESLKDGVFTTS-SDMWSFGVVLWeITSLAEQPYQGLSNEQVLKFVMDGGYlDQPDNCPER 249
                        250       260
                 ....*....|....*....|....
gi 375493532 236 SILLLQQMLQVDPKKRISMKNLLN 259
Cdd:cd05061  250 VTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
11-209 3.67e-10

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: 60.81  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  11 YELHETIGTGGFAKVKLACHILTGEMVAIKIMDkntlgSDLPR--IKTEIEALKNLRHQ-HICQLYHV--LETANKIFMV 85
Cdd:cd14130    2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVES-----AQQPKqvLKMEVAVLKKLQGKdHVCRFIGCgrNEKFNYVVMQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEycpGGELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENL----LFDEYHKLKLIDFGLCAK--- 156
Cdd:cd14130   77 LQ---GRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQytn 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 157 -------PKGNKDYHlqtccGSLAYAAPELIQGKSyLGSEADVWSMGILLYVLMCGFLPF 209
Cdd:cd14130  154 ttgevrpPRNVAGFR-----GTVRYASVNAHKNRE-MGRHDDLWSLFYMLVEFAVGQLPW 207
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
15-204 4.11e-10

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 61.22  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKVKLAchILTGEMVAIKIMdkntlgsdLPRIKT------EIEALKNLRHQHICQLYHVLETANKI-----F 83
Cdd:cd14054    1 QLIGQGRYGTVWKG--SLDERPVAVKVF--------PARHRQnfqnekDIYELPLMEHSNILRFIGADERPTADgrmeyL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  84 MVLEYCPGGELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQ---------GYAHRDLKPENLLFDEYHKLKLIDFGLC 154
Cdd:cd14054   71 LVLEYAPKGSLCSYL-RENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLA 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375493532 155 AKPKGNKDYHLQTC---------CGSLAYAAPELIQG-------KSYLgSEADVWSMGILLY-VLMC 204
Cdd:cd14054  150 MVLRGSSLVRGRPGaaenasiseVGTLRYMAPEVLEGavnlrdcESAL-KQVDVYALGLVLWeIAMR 215
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
13-203 4.25e-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: 60.65  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  13 LHETIGTGGFAKVKLACHILTGEM---VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYC 89
Cdd:cd05066    8 IEKVIGAGEFGEVCSGRLKLPGKReipVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  90 PGGELFDYIISQD-RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTC 168
Cdd:cd05066   88 ENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTR 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 375493532 169 CGSLA--YAAPELIQGKSYlGSEADVWSMGILLYVLM 203
Cdd:cd05066  168 GGKIPirWTAPEAIAYRKF-TSASDVWSYGIVMWEVM 203
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
5-263 4.40e-10

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: 61.57  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   5 DELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMdKNTLgSDLPRIKTEIEALKNLRHQ------HICQLYHVLET 78
Cdd:cd14226    9 EKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII-KNKK-AFLNQAQIEVRLLELMNKHdtenkyYIVRLKRHFMF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  79 ANKIFMVLE---YcpggELFDYIISQDR--LSEEETRVVFRQIVSAVAYVHSQGYA--HRDLKPENLLFDEYHK--LKLI 149
Cdd:cd14226   87 RNHLCLVFEllsY----NLYDLLRNTNFrgVSLNLTRKFAQQLCTALLFLSTPELSiiHCDLKPENILLCNPKRsaIKII 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 150 DFGLCAKPkGNKDYH-LQtccgSLAYAAPELIQGKSYlGSEADVWSMGILLYVLMCGFLPFDDDNVMA------------ 216
Cdd:cd14226  163 DFGSSCQL-GQRIYQyIQ----SRFYRSPEVLLGLPY-DLAIDMWSLGCILVEMHTGEPLFSGANEVDqmnkivevlgmp 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 217 -------------LYKKIMRGKY------DVPKWLSPSS-----IL---------------------------LLQQMLQ 245
Cdd:cd14226  237 pvhmldqapkarkFFEKLPDGTYylkktkDGKKYKPPGSrklheILgvetggpggrragepghtvedylkfkdLILRMLD 316
                        330
                 ....*....|....*...
gi 375493532 246 VDPKKRISMKNLLNHPWI 263
Cdd:cd14226  317 YDPKTRITPAEALQHSFF 334
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
7-203 5.04e-10

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 60.74  E-value: 5.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532   7 LLKYYELH--ETIGTGGFAKVKLACHILTGEM----VAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETAN 80
Cdd:cd05111    3 IFKETELRklKVLGSGVFGTVHKGIWIPEGDSikipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  81 kIFMVLEYCPGGELFDYIiSQDRLSEEETRVV--FRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLC-AKP 157
Cdd:cd05111   83 -LQLVTQLLPLGSLLDHV-RQHRGSLGPQLLLnwCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAdLLY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 375493532 158 KGNKDYHLQTCCGSLAYAAPELIQGKSYLgSEADVWSMGILLYVLM 203
Cdd:cd05111  161 PDDKKYFYSEAKTPIKWMALESIHFGKYT-HQSDVWSYGVTVWEMM 205
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
15-203 5.71e-10

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: 60.85  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  15 ETIGTGGFAKV---KLAcHILTG--EMVAIKIMDKNTLGSdlPRIKTEIEALKNLRHQHICQLY----HVLETANKIFMV 85
Cdd:cd14055    1 KLVGKGRFAEVwkaKLK-QNASGqyETVAVKIFPYEEYAS--WKNEKDIFTDASLKHENILQFLtaeeRGVGLDRQYWLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  86 LEYCPGGELFDYIiSQDRLSEEETRVVFRQIVSAVAYVHSQGY---------AHRDLKPENLLFDEYHKLKLIDFGLCAK 156
Cdd:cd14055   78 TAYHENGSLQDYL-TRHILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCVLADFGLALR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 375493532 157 --PKGNKDyHLQTC--CGSLAYAAPELIQGKSYLGS-----EADVWSMGILLYVLM 203
Cdd:cd14055  157 ldPSLSVD-ELANSgqVGTARYMAPEALESRVNLEDlesfkQIDVYSMALVLWEMA 211
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
12-251 6.25e-10

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: 60.78  E-value: 6.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  12 ELHETIGTGGFAKVKLACHILTGEMV--AIKIMDKNTLGSDLPRIKTEIEALKNL-RHQHICQLYHVLETANKIFMVLEY 88
Cdd:cd05089    5 KFEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532  89 CPGGELFDYIiSQDRLSEEE-------------TRVVFRQIVSAVA----YVHSQGYAHRDLKPENLLFDEYHKLKLIDF 151
Cdd:cd05089   85 APYGNLLDFL-RKSRVLETDpafakehgtastlTSQQLLQFASDVAkgmqYLSEKQFIHRDLAARNVLVGENLVSKIADF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493532 152 GLcakPKGNKDYHLQTcCGSLA--YAAPELIQGKSYLgSEADVWSMGILLY-VLMCGFLPFDDDNVMALYKKIMRG-KYD 227
Cdd:cd05089  164 GL---SRGEEVYVKKT-MGRLPvrWMAIESLNYSVYT-TKSDVWSFGVLLWeIVSLGGTPYCGMTCAELYEKLPQGyRME 238
                        250       260
                 ....*....|....*....|....
gi 375493532 228 VPKWLSPSSILLLQQMLQVDPKKR 251
Cdd:cd05089  239 KPRNCDDEVYELMRQCWRDRPYER 262
 
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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