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Conserved domains on  [gi|1398130438|ref|NP_001351076|]
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casein kinase I isoform gamma-3 isoform 14 [Homo sapiens]

Protein Classification

casein kinase I( domain architecture ID 10392958)

casein kinase I 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
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
1-215 1.68e-174

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14126:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 288  Bit Score: 484.24  E-value: 1.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14126    73 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYI 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14126   153 DPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 215
Cdd:cd14126   233 EVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
215-272 4.56e-19

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


:

Pssm-ID: 463640  Cd Length: 99  Bit Score: 80.69  E-value: 4.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 215 KQLPTPVGAVQ-QDPALSSNREAHQHRDKM----------QQSKN------------------------------QVVSS 253
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRPplpqprrvsqQGSKGrkgawppptpqtnaetlgshlpadrhggsvQVVSS 80
                          90
                  ....*....|....*....
gi 1398130438 254 TNGELNTDDPTAGRSNAPI 272
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
 
Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
1-215 1.68e-174

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 484.24  E-value: 1.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14126    73 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYI 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14126   153 DPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 215
Cdd:cd14126   233 EVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1-138 1.17e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 94.69  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 79
Cdd:COG0515    84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-----RVKLIDFGIARAL 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  80 IDPETKkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:COG0515   158 GGATLT------QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG 210
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-161 1.78e-20

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 88.36  E-value: 1.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438    1 MVLELLgpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:smart00220  74 LVMEYC--EGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-----VKLADFGLARQ 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   79 YIDPETkkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRAT 158
Cdd:smart00220 147 LDPGEK--------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPF 216

                   ...
gi 1398130438  159 PIE 161
Cdd:smart00220 217 PPP 219
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
29-195 9.55e-20

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 87.31  E-value: 9.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIdpETKKHIPY-REHKSL-TGTARYMSIN 106
Cdd:PHA02882  131 IMKDMLTTLEYIHEHGISHGDIKPENIMV-----DGNNRGYIIDYGIASHFI--IHGKHIEYsKEQKDLhRGTLYYAGLD 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 107 THLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE-MATYLRYVRRLDFFEK 185
Cdd:PHA02882  204 AHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKfIYDFIECVTKLSYEEK 283
                         170
                  ....*....|
gi 1398130438 186 PDYDYLRKLF 195
Cdd:PHA02882  284 PDYDALIKIF 293
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
215-272 4.56e-19

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


Pssm-ID: 463640  Cd Length: 99  Bit Score: 80.69  E-value: 4.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 215 KQLPTPVGAVQ-QDPALSSNREAHQHRDKM----------QQSKN------------------------------QVVSS 253
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRPplpqprrvsqQGSKGrkgawppptpqtnaetlgshlpadrhggsvQVVSS 80
                          90
                  ....*....|....*....
gi 1398130438 254 TNGELNTDDPTAGRSNAPI 272
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
22-138 4.47e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 54.03  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidPETkkhipyrehkSLT---- 97
Cdd:NF033483  105 SPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR-----VKVTDFGIARAL--SST----------TMTqtns 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  98 --GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 138
Cdd:NF033483  168 vlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1-87 1.13e-06

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 49.03  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE- 78
Cdd:pfam07714  78 IVTEYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL-----VVKISDFGLSRDi 152

                  ....*....
gi 1398130438  79 YIDPETKKH 87
Cdd:pfam07714 153 YDDDYYRKR 161
 
Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
1-215 1.68e-174

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 484.24  E-value: 1.68e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14126    73 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYI 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14126   153 DPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 232
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 215
Cdd:cd14126   233 EVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
1-195 3.11e-130

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: 371.02  E-value: 3.11e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYI 80
Cdd:cd14016    73 MVMDLLGPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNK--VYLIDFGLAKKYR 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14016   151 DPRTGKHIPYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSP 230
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLF 195
Cdd:cd14016   231 EELCKGLPkEFAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
1-204 3.10e-124

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: 356.29  E-value: 3.10e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpGNKTQQViHIIDFGLAKEYI 80
Cdd:cd14125    73 MVMDLLGPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGL-GKKGNLV-YIIDFGLAKKYR 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14125   151 DPRTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPI 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGY 204
Cdd:cd14125   231 EVLCKGFPsEFATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
1-203 1.26e-117

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 339.85  E-value: 1.26e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14127    73 LVIDLLGPSLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTKNANVIHVVDFGMAKQYR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPI 160
Cdd:cd14127   153 DPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPI 232
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1398130438 161 EVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKG 203
Cdd:cd14127   233 RDLCEGFPeEFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
1-195 9.68e-95

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: 281.32  E-value: 9.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL--IGRPGNKtqqvIHIIDFGLAKE 78
Cdd:cd14128    73 LVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLmgIGRHCNK----LFLIDFGLAKK 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 YIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRAT 158
Cdd:cd14128   149 YRDSRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMST 228
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1398130438 159 PIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLF 195
Cdd:cd14128   229 PVEVLCKGFPaEFAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
1-196 1.82e-54

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: 178.22  E-value: 1.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLF-DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLAKEY 79
Cdd:cd14017    73 IVMTLLGPNLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERT-VYILDFGLARQY 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  80 IDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKadtlkeRYQKIGDTKRATP 159
Cdd:cd14017   152 TNKDGEVERPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKID 225
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1398130438 160 IEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFT 196
Cdd:cd14017   226 HEELLKGLPkEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
1-195 2.04e-40

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 142.80  E-value: 2.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14015   104 LVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLG--FGKNKDQVYLVDYGLASRYC 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DpeTKKHIPYRE--HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIgdtKRAT 158
Cdd:cd14015   182 P--NGKHKEYKEdpRKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWEDNLKNPEYVQKQKE---KYMD 256
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1398130438 159 PI-EVLCENFP------EMATYLRYVRRLDFFEKPDYDYLRKLF 195
Cdd:cd14015   257 DIpLLLKKCFPgkdvpeELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
1-200 2.84e-29

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: 112.45  E-value: 2.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLAKEY 79
Cdd:cd14129    73 VVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKC-YMLDFGLARQF 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  80 IDPETKKHIPyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATP 159
Cdd:cd14129   152 TNSCGDVRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYE 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 160 IEVLCENF-PEMATYLRYVRRLDFFEKPDYdylrKLFTDLFD 200
Cdd:cd14129   225 HRLMLKHLpPEFSVFLDHISGLDYFTKPDY----QLLVSVFD 262
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
1-195 2.29e-28

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: 110.12  E-value: 2.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNkTQQVIHIIDFGLAKEY 79
Cdd:cd14130    73 VVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPS-TYRKCYMLDFGLARQY 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  80 IDpETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATP 159
Cdd:cd14130   152 TN-TTGEVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK------EQVGMIKEKYE 224
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1398130438 160 IEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLF 195
Cdd:cd14130   225 HRMLLKHMPsEFHLFLDHIASLDYFTKPDYQLIMSVF 261
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
1-195 8.09e-27

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024 [Multi-domain]  Cd Length: 301  Bit Score: 106.89  E-value: 8.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14122   104 MIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLS---YKNPDQVYLVDYGLAYRYC 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 D---PETKKHIPYREHKsltGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIgdTKRA 157
Cdd:cd14122   181 PegvHKEYKEDPKRCHD---GTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWEDNLKDPNYVRDSKI--RYRD 255
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1398130438 158 TPIEVLCENFP------EMATYLRYVRRLDFFEKPDYDYLRKLF 195
Cdd:cd14122   256 NISELMEKCFPgknkpgEIRKYMETVKLLGYTEKPLYPHLREIL 299
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
1-196 5.24e-24

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025 [Multi-domain]  Cd Length: 302  Bit Score: 99.15  E-value: 5.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnKTQQVIHIIDFGLAKEYI 80
Cdd:cd14123   106 MVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY---RNPNEVYLADYGLSYRYC 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 dpETKKHIPYREH--KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW----------QGLKADTLKERY 148
Cdd:cd14123   183 --PNGNHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeqnlknpvavQEAKAKLLSNLP 260
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438 149 QKIgdTKRATPIEVLCenfpEMATYLRYVRRLDFFEKPDYDYLRKLFT 196
Cdd:cd14123   261 DSV--LKWSTGGSSSM----EIAQFLSRVKDLAYDEKPDYQALKKILS 302
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
1-193 7.23e-24

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 98.76  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQqvIHIIDFGLAKEYI 80
Cdd:cd14124    99 LVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFV-DPEDQSE--VYLAGYGFAFRYC 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 dpETKKHIPYRE-HKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADT-----LKERY-QKIG 152
Cdd:cd14124   176 --PGGKHVEYREgSRSPhEGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHNTedimkQKERFmDDVP 253
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438 153 DT-----KRATPIEVLCEnfpematYLRYVRRLDFFEKPDYDYLRK 193
Cdd:cd14124   254 GFlgpcfHQKKVSEALQK-------YLKVVMALQYEEKPDYAMLRN 292
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1-129 2.95e-23

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: 95.03  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd00180    68 LVMEYCeGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT-----VKLADFGLAKDL 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  80 IDPETKKHIPYRehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYF 129
Cdd:cd00180   143 DSDDSLLKTTGG-----TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1-138 1.17e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 94.69  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 79
Cdd:COG0515    84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-----RVKLIDFGIARAL 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  80 IDPETKkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:COG0515   158 GGATLT------QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG 210
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
1-138 8.67e-21

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: 89.57  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 79
Cdd:cd14014    77 IVMEYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR-----VKLTDFGIARA- 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  80 IDPETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14014   150 LGDSGLTQT-----GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDG 203
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-161 1.78e-20

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 88.36  E-value: 1.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438    1 MVLELLgpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:smart00220  74 LVMEYC--EGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-----VKLADFGLARQ 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   79 YIDPETkkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRAT 158
Cdd:smart00220 147 LDPGEK--------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPF 216

                   ...
gi 1398130438  159 PIE 161
Cdd:smart00220 217 PPP 219
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
29-195 9.55e-20

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 87.31  E-value: 9.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIdpETKKHIPY-REHKSL-TGTARYMSIN 106
Cdd:PHA02882  131 IMKDMLTTLEYIHEHGISHGDIKPENIMV-----DGNNRGYIIDYGIASHFI--IHGKHIEYsKEQKDLhRGTLYYAGLD 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 107 THLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE-MATYLRYVRRLDFFEK 185
Cdd:PHA02882  204 AHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKfIYDFIECVTKLSYEEK 283
                         170
                  ....*....|
gi 1398130438 186 PDYDYLRKLF 195
Cdd:PHA02882  284 PDYDALIKIF 293
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
215-272 4.56e-19

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


Pssm-ID: 463640  Cd Length: 99  Bit Score: 80.69  E-value: 4.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 215 KQLPTPVGAVQ-QDPALSSNREAHQHRDKM----------QQSKN------------------------------QVVSS 253
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRPplpqprrvsqQGSKGrkgawppptpqtnaetlgshlpadrhggsvQVVSS 80
                          90
                  ....*....|....*....
gi 1398130438 254 TNGELNTDDPTAGRSNAPI 272
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1-151 4.55e-18

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: 81.79  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GpsleDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:cd05123    70 LVLDYVpgG----ELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH-----IKLTDFGLA 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  77 KEYIDPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 151
Cdd:cd05123   141 KELSSDGDRTY-------TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVL-LYeMLTGKPPFY---AENRKEIYEKI 205
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
1-211 1.50e-16

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: 78.03  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK- 77
Cdd:cd05581    78 FVLEYApnGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH-----IKITDFGTAKv 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  78 ---------EYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERY 148
Cdd:cd05581   151 lgpdsspesTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRG---SNEYLTF 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438 149 QKIgdTKRATPIevlCENFPEMAtylryvrrLDFFEKpdydylrKLFTDLFDRKGYMFDYEYD 211
Cdd:cd05581   228 QKI--VKLEYEF---PENFPPDA--------KDLIQK-------LLVLDPSKRLGVNENGGYD 270
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-205 1.14e-14

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: 72.85  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDpetkkhipyrEHKSLTG 98
Cdd:cd05612    96 GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH-----IKLTDFGFAKKLRD----------RTWTLCG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  99 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIgdtkratpievlcenfpeMATYLRYVR 178
Cdd:cd05612   161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD---DNPFGIYEKI------------------LAGKLEFPR 219
                         170       180
                  ....*....|....*....|....*...
gi 1398130438 179 RLDFFEKpdyDYLRKLFT-DLFDRKGYM 205
Cdd:cd05612   220 HLDLYAK---DLIKKLLVvDRTRRLGNM 244
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
12-233 3.30e-14

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: 71.46  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYIDPETkkhip 89
Cdd:cd05580    87 ELFSLLRRSgrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH-----IKITDFGFAK-RVKDRT----- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  90 yrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKI--GDTKratpievlcenF 167
Cdd:cd05580   156 ----YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF---FDENPMKIYEKIleGKIR-----------F 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 168 PEmatylryvrrldFFEKPDYDYLRKLFT-DLFDRKGYM-----------FDYEYDWIG---KQLPTPVGAVQQDPALSS 232
Cdd:cd05580   218 PS------------FFDPDAKDLIKRLLVvDLTKRLGNLkngvediknhpWFAGIDWDAllqRKIPAPYVPKVRGPGDTS 285

                  .
gi 1398130438 233 N 233
Cdd:cd05580   286 N 286
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1-83 4.34e-14

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: 70.73  E-value: 4.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYI 80
Cdd:cd05118    78 LVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI----NLELGQLKLADFGLARSFT 153

                  ...
gi 1398130438  81 DPE 83
Cdd:cd05118   154 SPP 156
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
32-151 6.77e-14

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: 70.33  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKeYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd05572   101 CVVLAFEYLHSRGIIYRDLKPENLLLDSNG-----YVKLVDFGFAK-KLGSGRKTW-------TFCGTPEYVAPEIILNK 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKeRYQKI 151
Cdd:cd05572   168 GYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMK-IYNII 206
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1-151 8.34e-14

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: 69.81  E-value: 8.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GpsleDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLA 76
Cdd:cd05117    76 LVMELCtgG----ELFDrIVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDS--PIKIIDFGLA 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  77 KEYIDPEtkkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMYF-LRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd05117   150 KIFEEGE--------KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLG-VILYIlLCGYPPFYG---ETEQELFEKI 213
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1-151 1.71e-12

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: 65.96  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAke 78
Cdd:cd14007    77 LILEYA--PNGELYKELKKQkrFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG-----SNGELKLADFGWS-- 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  79 yidpetkKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKI 151
Cdd:cd14007   148 -------VHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLG-VLCYeLLVGKPPF---ESKSHQETYKRI 210
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
1-104 1.77e-12

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: 66.02  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd13999    67 IVTEYMpGGSLYDLLHKKKIPLSWSLRLKIALD-IARgMNYLHSPPIIHRDLKSLNILLDENFT-----VKIADFGLSRI 140
                          90       100
                  ....*....|....*....|....*.
gi 1398130438  79 YIDPETKKhipyrehKSLTGTARYMS 104
Cdd:cd13999   141 KNSTTEKM-------TGVVGTPRWMA 159
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-194 2.25e-12

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: 66.16  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYIDPET 84
Cdd:cd13996    88 GGTLRDWIDRRNSSSKNdrKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL----DNDDLQVKIGDFGLATSIGNQKR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  85 KKHIP-------YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFLRgslpwqglkaDTLKERYQKIGDTK 155
Cdd:cd13996   164 ELNNLnnnnngnTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILfeMLHPF----------KTAMERSTILTDLR 233
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1398130438 156 RATPIEVLCENFPEMATYLRYVRRLDFFEKPD-YDYLRKL 194
Cdd:cd13996   234 NGILPESFKAKHPKEADLIQSLLSKNPEERPSaEQLLRSL 273
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
15-164 3.20e-12

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: 65.42  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  15 DLCD-----RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI----GRPGNKTQQVIHIIDFGLAKeYIDPETK 85
Cdd:cd14202    87 DLADylhtmRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIADFGFAR-YLQNNMM 165
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  86 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLC 164
Cdd:cd14202   166 A-------ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSS 237
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
32-162 4.43e-12

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: 64.98  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidpetkKHIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd14116   113 ELANALSYCHSKRVIHRDIKPENLLLGSAGE-----LKIADFGWS---------VHAPSSRRTTLCGTLDYLPPEMIEGR 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATPIEV 162
Cdd:cd14116   179 MHDEKVDLWSLGVLCYEFLVGKPPFE---ANTYQETYKRISRVEFTFPDFV 226
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1-79 8.69e-12

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: 64.43  E-value: 8.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 79
Cdd:cd07829    75 LVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG-----VLKLADFGLARAF 148
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
32-159 9.94e-12

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: 64.73  E-value: 9.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd05582   105 ELALALDHLHSLGIIYRDLKPENILLDEDGH-----IKLTDFGLSKESIDHEKKAY-------SFCGTVEYMAPEVVNRR 172
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGDTKRATP 159
Cdd:cd05582   173 GHTQSADWWSFGVLMFEMLTGSLPFQG---KDRKETMTMILKAKLGMP 217
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1-151 1.08e-11

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: 63.69  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14003    76 LVMEYA--SGGELFDYIvnNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN-----LKIIDFGLSNE 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  79 YidpetkkhIPYREHKSLTGTARYMS---INTH--LGKEQsrrdDLEALGHMfMYF-LRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd14003   149 F--------RGGSLLKTFCGTPAYAApevLLGRkyDGPKA----DVWSLGVI-LYAmLTGYLPFDD---DNDSKLFRKI 211
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
30-136 1.36e-11

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: 63.48  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKkhIPYREHKSLTGTARYMS---IN 106
Cdd:cd06626   105 TLQLLEGLAYLHENGIVHRDIKPANIFLDSNG-----LIKLGDFGSAVKLKNNTTT--MAPGEVNSLVGTPAYMApevIT 177
                          90       100       110
                  ....*....|....*....|....*....|
gi 1398130438 107 THLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06626   178 GNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
pknD PRK13184
serine/threonine-protein kinase PknD;
15-162 1.77e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.79  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  15 DLCDRTfSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqQVIhIIDFGLAK-----EYIDPETKKHIP 89
Cdd:PRK13184  105 ELAEKT-SVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVV-ILDWGAAIfkkleEEDLLDIDVDER 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  90 YREHKSLT------GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkadtlKERYQKIGDTKR-ATPIEV 162
Cdd:PRK13184  179 NICYSSMTipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR-------RKKGRKISYRDViLSPIEV 251
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
1-161 2.96e-11

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: 62.57  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 78
Cdd:cd14008    83 LVLEYCegGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG-----TVKISDFGVSEM 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 YIDPETkkhipyrEHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKIGDTK 155
Cdd:cd14008   158 FEDGND-------TLQKTAGTPAFLApelCDGDSKTYSGKAADIWALGVTLYCLVFGRLPF---NGDNILELYEAIQNQN 227

                  ....*.
gi 1398130438 156 RATPIE 161
Cdd:cd14008   228 DEFPIP 233
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
18-136 7.32e-11

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: 61.95  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 97
Cdd:cd05595    89 ERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH-----IKITDFGLCKEGITDGATM-------KTFC 156
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398130438  98 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05595   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1-133 9.80e-11

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: 61.19  E-value: 9.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 80
Cdd:cd07832    77 LVFEYMLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG-----VLKIADFGLARLFS 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  81 DPETKkhiPYREHkslTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGS 133
Cdd:cd07832   152 EEDPR---LYSHQ---VATRWYRAPELLYGSRKyDEGVDLWAVGCIFAELLNGS 199
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
30-136 1.54e-10

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: 60.23  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPETKKhipyrEHKSLTGTARYMS---IN 106
Cdd:cd06606   105 TRQILEGLEYLHSNGIVHRDIKGANILVD-----SDGVVKLADFGCAKRLAEIATGE-----GTKSLRGTPYWMApevIR 174
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1398130438 107 thlGKEQSRRDDLEALG----HMFMyflrGSLPW 136
Cdd:cd06606   175 ---GEGYGRAADIWSLGctviEMAT----GKPPW 201
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
30-151 1.66e-10

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: 60.57  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyiDPETKKHipyreHKSLTGTARYMSINTHL 109
Cdd:cd05611   103 IAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH-----LKLTDFGLSR---NGLEKRH-----NKKFVGTPDYLAPETIL 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 151
Cdd:cd05611   170 GVGDDKMSDWWSLGCVIFEFLFGYPPFH---AETPDAVFDNI 208
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
1-74 2.88e-10

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: 59.59  E-value: 2.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438   1 MVLELLGPSLEDLFDLcDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvIHIIDFG 74
Cdd:cd14133    78 IVFELLSQNLYEFLKQ-NKFqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ---IKIIDFG 149
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
12-104 3.37e-10

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: 59.67  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLC--DRTFSLKTVLM--IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqVIHIIDFGLAkeyidpeTKKH 87
Cdd:cd13993    91 DLFEAIteNRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG----TVKLCDFGLA-------TTEK 159
                          90
                  ....*....|....*..
gi 1398130438  88 IPYrehKSLTGTARYMS 104
Cdd:cd13993   160 ISM---DFGVGSEFYMA 173
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
12-123 3.53e-10

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: 59.19  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyidpetkkhIP 89
Cdd:cd14002    85 ELFQILedDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGG-----VVKLCDFGFARA---------MS 150
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1398130438  90 YREH--KSLTGTARYMSinTHLGKEQ--SRRDDLEALG 123
Cdd:cd14002   151 CNTLvlTSIKGTPLYMA--PELVQEQpyDHTADLWSLG 186
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
1-151 3.70e-10

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: 59.73  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDL--FDLCDRTFSLktvlmiaiqlisrmEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd05584    89 MHLEREGIFMEDTacFYLAEITLAL--------------GHLHSLGIIYRDLKPENILLDAQGH-----VKLTDFGLCKE 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  79 YIDPETKKHipyrehkSLTGTARYMS--INTHLGkeQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 151
Cdd:cd05584   150 SIHDGTVTH-------TFCGTIEYMApeILTRSG--HGKAVDWWSLGAL-MYdMLTGAPPFT---AENRKKTIDKI 212
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
32-151 8.07e-10

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: 58.38  E-value: 8.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKH--------IPYREHKSLTGTARYM 103
Cdd:cd05579   101 EIVLALEYLHSHGIIHRDLKPDNILIDANGH-----LKLTDFGLSKVGLVRRQIKLsiqkksngAPEKEDRRIVGTPDYL 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438 104 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd05579   176 APEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHA---ETPEEIFQNI 220
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
38-151 1.67e-09

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: 58.06  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  38 EYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID------------------PETKKHIPYREHK----S 95
Cdd:cd05573   115 DSLHKLGFIHRDIKPDNILLDADGH-----IKLADFGLCTKMNKsgdresylndsvntlfqdNVLARRRPHKQRRvrayS 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  96 LTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPwqgLKADTLKERYQKI 151
Cdd:cd05573   190 AVGTPDYIAPEVLRGTGYGPECDWWSLG-VILYeMLYGFPP---FYSDSLVETYSKI 242
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-186 1.80e-09

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: 57.58  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSlkTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKKHI-----PYRE 92
Cdd:cd14048   114 SRELF--VCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFF-----SLDDVVKVGDFGLVTAMDQGEPEQTVltpmpAYAK 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  93 HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLrgslpwqgLKADTLKERYQKIGDTKRATPIEVLCENFPEMAT 172
Cdd:cd14048   187 HTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI--------YSFSTQMERIRTLTDVRKLKFPALFTNKYPEERD 258
                         170
                  ....*....|....
gi 1398130438 173 YLRYVRRLDFFEKP 186
Cdd:cd14048   259 MVQQMLSPSPSERP 272
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
12-150 1.90e-09

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: 57.32  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKhIP 89
Cdd:cd13994    84 DLFTLIekADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG-----VLKLTDFGTAEVFGMPAEKE-SP 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  90 YRehKSLTGTARYMSINTHLGKEQS-RRDDLEALGHMFMYFLRGSLPWQglKADTLKERYQK 150
Cdd:cd13994   158 MS--AGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWR--SAKKSDSAYKA 215
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
32-151 1.92e-09

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 57.91  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyidpetkkhIPYREHkSLTGTARYMSINTHLGK 111
Cdd:PTZ00263  126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGH-----VKVTDFGFAKK---------VPDRTF-TLCGTPEYLAPEVIQSK 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:PTZ00263  191 GHGKAVDWWTMGVLLYEFIAGYPPFFD---DTPFRIYEKI 227
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1-151 2.03e-09

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: 57.18  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14099    78 ILLELC--SNGSLMELLKRrkALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN-----VKIGDFGLAAR 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  79 yIDPETKKhipyreHKSLTGTARYMS--InthLGKEQ--SRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 151
Cdd:cd14099   151 -LEYDGER------KKTLCGTPNYIApeV---LEKKKghSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRI 214
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
18-138 2.06e-09

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: 57.27  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidpeTKKHiPYREHKSLT 97
Cdd:cd05578    94 KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH-----VHITDFNIA-------TKLT-DGTLATSTS 160
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398130438  98 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd05578   161 GTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEI 201
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
26-166 2.63e-09

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: 56.94  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  26 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVihIIDFGLAKEYIDpetKKHIPyrehKSLTGTARYMSI 105
Cdd:cd13995    98 IIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF----MSTKAV--LVDFGLSVQMTE---DVYVP----KDLRGTEIYMSP 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438 106 NTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIgDTKRATPIEVLCEN 166
Cdd:cd13995   165 EVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYI-IHKQAPPLEDIAQD 224
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1-91 2.66e-09

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 56.77  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438    1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK- 77
Cdd:smart00219  78 IVMEYMeGGDLLSYLRKNRPKLSLSDLLSFALQ-IARgMEYLESKNFIHRDLAARNCLVGE-----NLVVKISDFGLSRd 151
                           90
                   ....*....|....*...
gi 1398130438   78 ----EYIDPETKKhIPYR 91
Cdd:smart00219 152 lyddDYYRKRGGK-LPIR 168
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
30-151 3.03e-09

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: 56.81  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHL 109
Cdd:cd05608   111 TAQIISGLEHLHQRRIIYRDLKPENVLLDDDGN-----VRISDLGLAVELKDGQTKT-------KGYAGTPGFMAPELLL 178
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFL--RGSLPWQGLKADTlKERYQKI 151
Cdd:cd05608   179 GEEYDYSVDYFTLGVTLYEMIaaRGPFRARGEKVEN-KELKQRI 221
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
1-104 3.06e-09

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: 56.59  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgPSLEdLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14093    86 LVFELC-RKGE-LFDYLTEvvTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN-----VKISDFGFATR 158
                          90       100
                  ....*....|....*....|....*.
gi 1398130438  79 yIDPETKkhipYREhksLTGTARYMS 104
Cdd:cd14093   159 -LDEGEK----LRE---LCGTPGYLA 176
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
1-151 3.72e-09

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: 56.53  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLEL-LGPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd14010    71 LVVEYcTGGDLETLLRQ-DGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGT-----LKLSDFGLARRE 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  80 ID---------PETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFlrGSLPWQglkADTLKERY 148
Cdd:cd14010   145 GEilkelfgqfSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLyeMFT--GKPPFV---AESFTELV 219

                  ...
gi 1398130438 149 QKI 151
Cdd:cd14010   220 EKI 222
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
13-146 3.99e-09

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: 56.38  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  13 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidPETKKhipyre 92
Cdd:cd05577    84 IYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH-----VRISDLGLAVEF--KGGKK------ 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  93 HKSLTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 146
Cdd:cd05577   151 IKGRVGTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKE 205
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1-77 4.01e-09

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: 56.56  E-value: 4.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 77
Cdd:cd07833    77 LVFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG-----VLKLCDFGFAR 148
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-74 4.80e-09

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: 56.40  E-value: 4.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   1 MVLELLGPSLEDLfdLCDRTF---SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQqvIHIIDFG 74
Cdd:cd14210    92 IVFELLSINLYEL--LKSNNFqglSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKSS--IKVIDFG 163
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
32-136 5.10e-09

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: 55.80  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyREHKSLTGTARYMSINThLGK 111
Cdd:cd14069   108 QLMAGLKYLHSCGITHRDIKPENLLLDENDN-----LKISDFGLATVFRYKGKE-----RLLNKMCGTLPYVAPEL-LAK 176
                          90       100
                  ....*....|....*....|....*..
gi 1398130438 112 EQSRRD--DLEALGHMFMYFLRGSLPW 136
Cdd:cd14069   177 KKYRAEpvDVWSCGIVLFAMLAGELPW 203
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1-91 5.64e-09

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: 55.63  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438    1 MVLELL-GPSLED-LFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:smart00221  78 IVMEYMpGGDLLDyLRKNRPKELSLSDLLSFALQ-IARgMEYLESKNFIHRDLAARNCLVGE-----NLVVKISDFGLSR 151
                           90
                   ....*....|....*....
gi 1398130438   78 E-----YIDPETKKhIPYR 91
Cdd:smart00221 152 DlydddYYKVKGGK-LPIR 169
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
1-76 6.22e-09

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: 56.42  E-value: 6.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLED-LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL--------IGRPGNKTQQV---- 67
Cdd:cd14134    91 IVFELLGPSLYDfLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkVYNPKKKRQIRvpks 170
                          90
                  ....*....|.
gi 1398130438  68 --IHIIDFGLA 76
Cdd:cd14134   171 tdIKLIDFGSA 181
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1-102 6.50e-09

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: 56.08  E-value: 6.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 80
Cdd:cd07843    83 MVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG-----ILKICDFGLAREYG 157
                          90       100
                  ....*....|....*....|....*...
gi 1398130438  81 DPeTKKHIP------YREHKSLTGTARY 102
Cdd:cd07843   158 SP-LKPYTQlvvtlwYRAPELLLGAKEY 184
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
29-149 6.55e-09

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: 55.79  E-value: 6.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnKTQQVIHIIDFGL---------AKEYIDP-------ETKKHIPYRE 92
Cdd:cd13987    96 CAAQLASALDFMHSKNLVHRDIKPENVLLFD---KDCRRVKLCDFGLtrrvgstvkRVSGTIPytapevcEAKKNEGFVV 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  93 HKSLtgtarymsinthlgkeqsrrdDLEALGHMFMYFLRGSLPWQglKADTLKERYQ 149
Cdd:cd13987   173 DPSI---------------------DVWAFGVLLFCCLTGNFPWE--KADSDDQFYE 206
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
18-136 6.56e-09

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: 56.13  E-value: 6.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 97
Cdd:cd05603    90 ERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH-----VVLTDFGLCKEGMEPEETT-------STFC 157
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398130438  98 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05603   158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
1-85 6.63e-09

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: 55.69  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFD-LCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqqvIHIIDFGLA 76
Cdd:cd14103    67 LVMEYVAGG--ELFErVVDDDFELteRDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQ----IKIIDFGLA 140

                  ....*....
gi 1398130438  77 KEYiDPETK 85
Cdd:cd14103   141 RKY-DPDKK 148
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-102 8.04e-09

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: 55.79  E-value: 8.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 80
Cdd:cd07871    80 LVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE-----LKLADFGLARAKS 154
                          90       100
                  ....*....|....*....|....*...
gi 1398130438  81 DPeTKKH------IPYREHKSLTGTARY 102
Cdd:cd07871   155 VP-TKTYsnevvtLWYRPPDVLLGSTEY 181
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
19-78 8.44e-09

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: 55.62  E-value: 8.44e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKE 78
Cdd:cd07830    94 KPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV-----SGPEVVKIADFGLARE 148
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
18-85 1.06e-08

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: 55.40  E-value: 1.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqviHII--DFGLAKEYIDPETK 85
Cdd:cd05575    90 ERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQG-------HVVltDFGLCKEGIEPSDT 152
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1-138 1.08e-08

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: 55.09  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLCDRTFSLK--TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTQQVIHIIDFGLAKe 78
Cdd:cd14084    88 IVLELMEGG--ELFDRVVSNKRLKeaICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLS--SQEEECLIKITDFGLSK- 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  79 yIDPETKKhipyreHKSLTGTARYMS--INTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14084   163 -ILGETSL------MKTLCGTPTYLApeVLRSFGTEGyTRAVDCWSLGVILFICLSGYPPFSE 218
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-126 1.11e-08

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: 55.39  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyi 80
Cdd:cd07873    77 LVFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLAR--- 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1398130438  81 dpetKKHIPYREHKSLTGTARYMSINTHLGK-EQSRRDDLEALGHMF 126
Cdd:cd07873   149 ----AKSIPTKTYSNEVVTLWYRPPDILLGStDYSTQIDMWGVGCIF 191
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
12-93 1.23e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 54.86  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQqvIHIIDFGLAK------------ 77
Cdd:PHA03390   95 DLFDLLkkEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR--AKDR--IYLCDYGLCKiigtpscydgtl 170
                          90
                  ....*....|....*.
gi 1398130438  78 EYIDPETKKHIPYREH 93
Cdd:PHA03390  171 DYFSPEKIKGHNYDVS 186
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
32-103 1.50e-08

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: 54.54  E-value: 1.50e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKeYIDPETKKHipyrehkSLTGTARYM 103
Cdd:cd14009   100 QLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDP--VLKIADFGFAR-SLQPASMAE-------TLCGSPLYM 161
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
17-123 1.66e-08

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: 54.35  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  17 CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYidpeTKKHIPYrehkSL 96
Cdd:cd08220    94 KGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL----NKKRTVVKIGDFGISKIL----SSKSKAY----TV 161
                          90       100
                  ....*....|....*....|....*..
gi 1398130438  97 TGTARYMSINTHLGKEQSRRDDLEALG 123
Cdd:cd08220   162 VGTPCYISPELCEGKPYNQKSDIWALG 188
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
20-161 1.76e-08

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: 54.63  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  20 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQV----IHIIDFGLAKeYIDPETKKhipyrehKS 95
Cdd:cd14201   101 TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVsgirIKIADFGFAR-YLQSNMMA-------AT 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  96 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIE 161
Cdd:cd14201   173 LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRE 238
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
32-159 1.98e-08

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: 54.16  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGK 111
Cdd:cd14189   109 QIISGLKYLHLKGILHRDLKLGNFFI----NENME-LKVGDFGLAARLEPPEQRK-------KTICGTPNYLAPEVLLRQ 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKadtLKERYQKIGDTKRATP 159
Cdd:cd14189   177 GHGPESDVWSLGCVMYTLLCGNPPFETLD---LKETYRCIKQVKYTLP 221
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
32-151 2.09e-08

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: 54.10  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidpeTKKHIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd14186   110 QIVTGMLYLHSHGILHRDLTLSNLLLTRNMN-----IKIADFGLA-------TQLKMPHEKHFTMCGTPNYISPEIATRS 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 151
Cdd:cd14186   178 AHGLESDVWSLGCMFYTLLVGRPPFD---TDTVKNTLNKV 214
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
18-80 2.23e-08

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: 54.67  E-value: 2.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 80
Cdd:cd05571    89 ERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGH-----IKITDFGLCKEEI 146
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
15-203 2.23e-08

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 54.60  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  15 DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPETKKhipyreh 93
Cdd:cd05103   170 DLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPDYVR------- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  94 kslTGTAR----YMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRAtpievlcenfP 168
Cdd:cd05103   238 ---KGDARlplkWMAPETIFDRVYTIQSDVWSFGvLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRA----------P 304
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1398130438 169 EMATYLRYVRRLDFFE-KPDYdylRKLFTDLFDRKG 203
Cdd:cd05103   305 DYTTPEMYQTMLDCWHgEPSQ---RPTFSELVEHLG 337
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-104 2.52e-08

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: 53.94  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  16 LCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqviHII--DFGLAKEYIDPETkkhipYRE 92
Cdd:cd05583    90 LYQREhFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEG-------HVVltDFGLSKEFLPGEN-----DRA 157
                          90
                  ....*....|..
gi 1398130438  93 HkSLTGTARYMS 104
Cdd:cd05583   158 Y-SFCGTIEYMA 168
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
1-82 2.74e-08

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: 53.80  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAkEY 79
Cdd:cd14119    73 MVMEYCVGGLQEMLDSApDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL-----TTDGTLKISDFGVA-EA 146

                  ...
gi 1398130438  80 IDP 82
Cdd:cd14119   147 LDL 149
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
30-151 3.12e-08

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: 54.27  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE------------TKKHIPYREHK--- 94
Cdd:cd05600   123 AISSLHQLGYIH------RDLKPENFLIDSSGH-----IKLTDFGLASGTLSPKkiesmkirleevKNTAFLELTAKerr 191
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  95 ---------------SLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd05600   192 niyramrkedqnyanSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG---STPNETWANL 260
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
27-195 3.12e-08

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: 53.65  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  27 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpETKKHIPYREHKsltGTARYMSIN 106
Cdd:cd14047   120 LEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK-----VKIGDFGLVT-----SLKNDGKRTKSK---GTLSYMSPE 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 107 THLGKEQSRRDDLEALGHMFMYFLRgslpwqglKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKP 186
Cdd:cd14047   187 QISSQDYGKEVDIYALGLILFELLH--------VCDSAFEKSKFWTDLRNGILPDIFDKRYKIEKTIIKKMLSKKPEDRP 258

                  ....*....
gi 1398130438 187 DYDYLRKLF 195
Cdd:cd14047   259 NASEILRTL 267
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
1-82 3.19e-08

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: 53.48  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDlcDRTFSLK-----TVLMIAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGL 75
Cdd:cd14095    75 LVMELV--KGGDLFD--AITSSTKfterdASRMVT-DLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSL-KLADFGL 148

                  ....*..
gi 1398130438  76 AKEYIDP 82
Cdd:cd14095   149 ATEVKEP 155
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
22-138 4.47e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 54.03  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidPETkkhipyrehkSLT---- 97
Cdd:NF033483  105 SPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR-----VKVTDFGIARAL--SST----------TMTqtns 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  98 --GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 138
Cdd:NF033483  168 vlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-202 4.49e-08

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: 53.81  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI---DPETkkhipyrehk 94
Cdd:cd05604    91 ERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH-----IVLTDFGLCKEGIsnsDTTT---------- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  95 SLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKR---ATPIEVLCENFPEMA 171
Cdd:cd05604   156 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRpgiSLTAWSILEELLEKD 235
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1398130438 172 TYLRYVRRLDFFEKPDYDYLRKL-FTDLFDRK 202
Cdd:cd05604   236 RQLRLGAKEDFLEIKNHPFFESInWTDLVQKK 267
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1-132 4.72e-08

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: 53.04  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDlCDRTFSL---KTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGL 75
Cdd:cd13982    72 IALELCAASLQDLVE-SPRESKLflrPGLEPVRLlrQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRAMISDFGL 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  76 AKEYidpETKKHiPYREHKSLTGT----ARYMsINTHLGKEQSRRDDLEALGHMFMYFLRG 132
Cdd:cd13982   151 CKKL---DVGRS-SFSRRSGVAGTsgwiAPEM-LSGSTKRRQTRAVDIFSLGCVFYYVLSG 206
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
15-150 4.72e-08

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: 53.14  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  15 DLCD-----RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNK----TQQVIHIIDFGLAKeYIDPETK 85
Cdd:cd14120    78 DLADylqakGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRkpspNDIRLKIADFGFAR-FLQDGMM 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  86 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 150
Cdd:cd14120   157 A-------ATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEK 214
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
12-82 4.78e-08

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: 53.03  E-value: 4.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  12 DLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLAKEYIDP 82
Cdd:cd14185    84 DLFDAIIESvkFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTT-LKLADFGLAKYVTGP 155
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
2-140 5.39e-08

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: 52.98  E-value: 5.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   2 VLELL-GPSLEDLFDLCdRTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 79
Cdd:cd06623    77 VLEYMdGGSLADLLKKV-GKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE-----VKIADFGISKV- 149
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  80 IDPETKKhipyreHKSLTGTARYMS---INthlGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 140
Cdd:cd06623   150 LENTLDQ------CNTFVGTVTYMSperIQ---GESYSYAADIWSLGLTLLECALGKFPFLPPG 204
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
1-104 5.43e-08

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: 52.66  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRTFSLkTVLMIAI---QLISRMEYVHSKNLIYRDVKPENFLI-GRPGNKtqqvIHIIDFGLA 76
Cdd:cd14006    66 LILELC--SGGELLDRLAERGSL-SEEEVRTymrQLLEGLQYLHNHHILHLDLKPENILLaDRPSPQ----IKIIDFGLA 138
                          90       100
                  ....*....|....*....|....*...
gi 1398130438  77 KEYIDPETKKHIpyrehkslTGTARYMS 104
Cdd:cd14006   139 RKLNPGEELKEI--------FGTPEFVA 158
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
29-147 5.62e-08

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: 52.86  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIHIIDFGLAKeYIDPETKKhipyrehKSLTGTARYMSINTH 108
Cdd:cd14098   106 LTKQILEAMAYTHSMGITHRDLKPENILITQDDPV---IVKISDFGLAK-VIHTGTFL-------VTFCGTMAYLAPEIL 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438 109 LGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKER 147
Cdd:cd14098   175 MSKEQNLQGgysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKR 219
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
14-146 5.81e-08

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: 53.41  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  14 FDLCDRTFslktvlmIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyreh 93
Cdd:cd05620    93 FDLYRATF-------YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-----IKIADFGMCKENVFGDNRA------- 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  94 KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 146
Cdd:cd05620   154 STFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFE 206
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
32-147 5.86e-08

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: 52.91  E-value: 5.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpetkkhIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd14072   107 QIVSAVQYCHQKRIVHRDLKAENLLLDADMN-----IKIADFGFSNEF--------TPGNKLDTFCGSPPYAAPELFQGK 173
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1398130438 112 EQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 147
Cdd:cd14072   174 KYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRER 210
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-136 5.88e-08

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: 53.48  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 97
Cdd:cd05602   102 ERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH-----IVLTDFGLCKENIEPNGTT-------STFC 169
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398130438  98 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05602   170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1-151 5.91e-08

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: 53.18  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 78
Cdd:cd14209    78 MVMEYVPGG--EMFSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQG-----YIKVTDFGFAKR 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  79 yIDPETkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 151
Cdd:cd14209   151 -VKGRT---------WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKI 210
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
1-135 6.97e-08

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: 52.60  E-value: 6.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd06614    73 VVMEYMdGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS-----VKLADFGFAAQL 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  80 idpeTKKHiPYRehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:cd06614   148 ----TKEK-SKR--NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
1-137 7.10e-08

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: 52.54  E-value: 7.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELlgPSLEDLFD--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAke 78
Cdd:cd14087    74 MVMEL--ATGGELFDriIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSK--IMITDFGLA-- 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  79 yidpETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14087   148 ----STRKKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD 202
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
21-144 7.91e-08

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: 52.77  E-value: 7.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIdpetkkhipYREHKSLT--G 98
Cdd:cd05592    93 FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH-----IKIADFGMCKENI---------YGENKASTfcG 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  99 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05592   159 TPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDEL 204
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-132 8.24e-08

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: 52.69  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyi 80
Cdd:cd07872    81 LVFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLAR--- 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  81 dpetKKHIPYREHKSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRG 132
Cdd:cd07872   153 ----AKSVPTKTYSNEVVTLWYRPPDVLLGsSEYSTQIDMWGVGCIFFEMASG 201
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
1-79 9.91e-08

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: 52.44  E-value: 9.91e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07839    76 LVFEYCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE-----LKLADFGLARAF 149
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
1-151 1.05e-07

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: 52.33  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLE-DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAke 78
Cdd:cd05630    77 LVLTLMnGGDLKfHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH-----IRISDLGLA-- 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  79 yidpetkKHIPYREH-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKI 151
Cdd:cd05630   150 -------VHVPEGQTiKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERL 216
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1-85 1.08e-07

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: 52.19  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 80
Cdd:cd07841    79 LVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDG-----VLKLADFGLARSFG 153

                  ....*
gi 1398130438  81 DPETK 85
Cdd:cd07841   154 SPNRK 158
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
29-135 1.54e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 52.13  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAK---EYIDPetkkhipyreHKSLTGTARYMS- 104
Cdd:PLN00034  173 VARQILSGIAYLHRRHIVHRDIKPSNLLI----NSAKNV-KIADFGVSRilaQTMDP----------CNSSVGTIAYMSp 237
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1398130438 105 --INTHL--GKEQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:PLN00034  238 erINTDLnhGAYDGYAGDIWSLGVSILEFYLGRFP 272
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
7-103 1.68e-07

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: 51.23  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKeyidpET 84
Cdd:cd13997    84 NGSLQDALEELSPISKLSEaeVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG-----TCKIGDFGLAT-----RL 153
                          90
                  ....*....|....*....
gi 1398130438  85 KKHIPYREhksltGTARYM 103
Cdd:cd13997   154 ETSGDVEE-----GDSRYL 167
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
32-162 1.74e-07

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: 51.13  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIHIIDFGLAKeYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd14121   103 QLASALQFLREHNISHMDLKPQNLLLSSRYNP---VLKLADFGFAQ-HLKPNDEAH-------SLRGSPLYMAPEMILKK 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438 112 EQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKIgdtKRATPIEV 162
Cdd:cd14121   172 KYDARVDLWSVG-VILYeCLFGRAPF---ASRSFEELEEKI---RSSKPIEI 216
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
29-136 1.76e-07

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: 51.58  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 107
Cdd:cd06605   104 IAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ-----VKLCDFGVSGQLVDSLA---------KTFVGTRSYMAPER 169
                          90       100
                  ....*....|....*....|....*....
gi 1398130438 108 HLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06605   170 ISGGKYTVKSDIWSLGLSLVELATGRFPY 198
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
14-144 1.79e-07

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: 51.85  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  14 FDLCDRTFslktvlmIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyreh 93
Cdd:cd05619   103 FDLPRATF-------YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-----IKIADFGMCKENMLGDAKT------- 163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  94 KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05619   164 STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEEL 214
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
18-146 1.95e-07

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: 51.62  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKkhipyrehKSL 96
Cdd:cd05593   109 ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-----IKITDFGLCKEGItDAATM--------KTF 175
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  97 TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 146
Cdd:cd05593   176 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 225
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
1-77 1.96e-07

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: 51.16  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFD-LCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHIIDFGLAK 77
Cdd:cd14191    76 MVLEMV--SGGELFErIIDEDFELteRECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC---VNKTGTKIKLIDFGLAR 150
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
11-137 2.40e-07

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: 50.98  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  11 EDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrPGNktqqVIHIIDFGLAKEYiDPETKKHIP 89
Cdd:cd14111    85 ELLHSLIDRfRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT-NLN----AIKIVDFGSAQSF-NPLSLRQLG 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  90 YRehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14111   159 RR-----TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE 201
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
7-125 2.41e-07

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: 50.95  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIhIIDFGLAKEYIDPETKK 86
Cdd:cd14065    72 GGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLV-REANRGRNAV-VADFGLAREMPDEKTKK 149
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398130438  87 hiPYR-EHKSLTGTARYMSINTHLGKEQSRRDDLEALGHM 125
Cdd:cd14065   150 --PDRkKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
18-136 2.78e-07

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: 51.18  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHS-KNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKkhipyrehKS 95
Cdd:cd05594   119 ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-----IKITDFGLCKEGIkDGATM--------KT 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398130438  96 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05594   186 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 226
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
29-152 2.85e-07

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: 50.63  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTH 108
Cdd:cd14164   105 MFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK----IKIADFGFARFVEDYPELST-------TFCGSRAYTPPEVI 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438 109 LG-KEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkeRYQKIG 152
Cdd:cd14164   174 LGtPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRG 216
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1-79 2.94e-07

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: 50.74  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEY 79
Cdd:cd07838    83 LVFEHVDQDLATYLDKCpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS-----DGQVKLADFGLARIY 157
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
30-201 3.42e-07

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: 50.81  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNL---IYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYidpetkkhipYREHK-SLTGTARY 102
Cdd:cd14145   110 AVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKvenGDLSNKILKITDFGLAREW----------HRTTKmSAAGTYAW 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 103 MSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLCenfPEmatylRYVRRLDF 182
Cdd:cd14145   180 MAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGI--DGLAVAY-GVAMNKLSLPIPSTC---PE-----PFARLMED 248
                         170
                  ....*....|....*....
gi 1398130438 183 FEKPDyDYLRKLFTDLFDR 201
Cdd:cd14145   249 CWNPD-PHSRPPFTNILDQ 266
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
21-136 3.65e-07

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: 51.07  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehkSLTGTA 100
Cdd:cd05614   102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH-----VVLTDFGLSKEFLTEEKERTY------SFCGTI 170
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1398130438 101 RYMSINTHLGKE-QSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05614   171 EYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPF 207
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
26-151 3.93e-07

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: 50.73  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  26 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYREHKSLTGTARYMSI 105
Cdd:cd07870   100 VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE-----LKLADFGLAR-------AKSIPSQTYSSEVVTLWYRPP 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1398130438 106 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLkADTLkERYQKI 151
Cdd:cd07870   168 DVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPGV-SDVF-EQLEKI 212
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
30-144 4.10e-07

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: 50.19  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPETKkhipyrehKSLTGTARYMSINTHL 109
Cdd:cd14059    87 SKQIASGMNYLHLHKIIHRDLKSPNVLVT-----YNDVLKISDFGTSKELSEKSTK--------MSFAGTVAWMAPEVIR 153
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 144
Cdd:cd14059   154 NEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAI 188
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
32-152 4.17e-07

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: 50.10  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA--KEYIDPETKKHipyrehkSLTGTARYMSinthl 109
Cdd:cd14663   108 QLIDAVDYCHSRGVFHRDLKPENLLLDEDGN-----LKISDFGLSalSEQFRQDGLLH-------TTCGTPNYVA----- 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438 110 gKEQSRRD-------DLEALGHMFMYFLRGSLPWQglkADTLKERYQKIG 152
Cdd:cd14663   171 -PEVLARRgydgakaDIWSCGVILFVLLAGYLPFD---DENLMALYRKIM 216
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
32-104 4.37e-07

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: 50.39  E-value: 4.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPetkkhIPYREHKSLTGTARYMS 104
Cdd:cd07866   123 QLLEGINYLHENHILHRDIKAANILIDNQG-----ILKIADFGLARPYDGP-----PPNPKGGGGGGTRKYTN 185
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
24-123 4.72e-07

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: 50.11  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  24 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYM 103
Cdd:cd06621   105 KVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ-----VKLCDFGVSGELVNSLA---------GTFTGTSYYM 170
                          90       100
                  ....*....|....*....|
gi 1398130438 104 SINTHLGKEQSRRDDLEALG 123
Cdd:cd06621   171 APERIQGGPYSITSDVWSLG 190
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
21-104 4.83e-07

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: 50.15  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKhipyrehKSLTGTA 100
Cdd:cd08215   100 FPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG-----VVKLGDFGISKVLESTTDLA-------KTVVGTP 167

                  ....
gi 1398130438 101 RYMS 104
Cdd:cd08215   168 YYLS 171
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
21-136 4.90e-07

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: 50.38  E-value: 4.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehkSLTGTA 100
Cdd:cd05613   102 FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGH-----VVLTDFGLSKEFLLDENERAY------SFCGTI 170
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1398130438 101 RYMSINTHLGKE--QSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05613   171 EYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLTGASPF 208
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1-90 4.99e-07

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: 50.38  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKE 78
Cdd:cd14166    77 LVMQLV--SGGELFDrILERgVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSK--IMITDFGLSKM 152
                          90       100
                  ....*....|....*....|....*.
gi 1398130438  79 --------------YIDPETKKHIPY 90
Cdd:cd14166   153 eqngimstacgtpgYVAPEVLAQKPY 178
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
30-87 6.09e-07

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: 49.75  E-value: 6.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYiDPETKKH 87
Cdd:cd14077   119 ARQIASALDYLHRNSIVHRDLKIENILISKSGN-----IKIIDFGLSNLY-DPRRLLR 170
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-137 7.38e-07

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: 50.04  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKe 78
Cdd:cd14179    79 LVMELLKGG--ELLERIKKKqhFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE--IKIIDFGFAR- 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  79 yIDPETKKHIpyrehKSLTGTARYMS--INTHLGKEQSRrdDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14179   154 -LKPPDNQPL-----KTPCFTLHYAApeLLNYNGYDESC--DLWSLGVILYTMLSGQVPFQ 206
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
12-95 7.57e-07

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: 49.56  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK------------ 77
Cdd:cd14081    87 ELFDyLVKKgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL-----DEKNNIKIADFGMASlqpegslletsc 161
                          90       100
                  ....*....|....*....|.
gi 1398130438  78 ---EYIDPETKKHIPYREHKS 95
Cdd:cd14081   162 gspHYACPEVIKGEKYDGRKA 182
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
32-193 8.75e-07

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: 49.45  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY----IDPETKKHIPyrehkSLTGTARYMSINT 107
Cdd:cd06628   114 QILKGLNYLHNRGIIHRDIKGANILVDNKGG-----IKISDFGISKKLeansLSTKNNGARP-----SLQGSVFWMAPEV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 108 HLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDTKRATPIEVLCEnfpEMATYLRYVRRLDFFEKPD 187
Cdd:cd06628   184 VKQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQAIF-KIGENASPTIPSNISS---EARDFLEKTFEIDHNKRPT 257

                  ....*.
gi 1398130438 188 YDYLRK 193
Cdd:cd06628   258 ADELLK 263
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
1-96 8.88e-07

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: 49.26  E-value: 8.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLEL--LGPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnktqQVIHIIDFGLAKE 78
Cdd:cd05040    74 MVTELapLGSLLDRLRKDQGH-FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASK-----DKVKIGDFGLMRA 147
                          90
                  ....*....|....*...
gi 1398130438  79 YidPETKKHIPYREHKSL 96
Cdd:cd05040   148 L--PQNEDHYVMQEHRKV 163
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
9-104 9.17e-07

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: 49.19  E-value: 9.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   9 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhi 88
Cdd:cd06612    84 SVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ-----AKLADFGVSGQLTDTMAKR-- 156
                          90
                  ....*....|....*.
gi 1398130438  89 pyrehKSLTGTARYMS 104
Cdd:cd06612   157 -----NTVIGTPFWMA 167
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
28-83 9.77e-07

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: 49.78  E-value: 9.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  28 MIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKeYIDPE 83
Cdd:cd07854   118 LFMYQLLRGLKYIHSANVLHRDLKPANVFI----NTEDLVLKIGDFGLAR-IVDPH 168
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
1-136 9.98e-07

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: 49.18  E-value: 9.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14200   102 MVFDLLrkGPVMEVP---SDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGH-----VKIADFGVSNQ 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  79 YIDPETkkhipyrEHKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd14200   174 FEGNDA-------LLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPF 227
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
1-157 1.04e-06

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: 49.24  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKE 78
Cdd:cd14178    74 LVMELMrGGELLDRI-LRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNP--ESIRICDFGFAKQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 yidpetkkhipYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIG 152
Cdd:cd14178   151 -----------LRAENGLLMTPCYTA--NFVAPEVLKRQgydaacDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIG 217

                  ....*
gi 1398130438 153 DTKRA 157
Cdd:cd14178   218 SGKYA 222
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
14-77 1.11e-06

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: 49.29  E-value: 1.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  14 FDLCDRT-----------FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:cd07847    79 FEYCDHTvlneleknprgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITK-----QGQIKLCDFGFAR 148
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1-87 1.13e-06

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 49.03  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE- 78
Cdd:pfam07714  78 IVTEYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL-----VVKISDFGLSRDi 152

                  ....*....
gi 1398130438  79 YIDPETKKH 87
Cdd:pfam07714 153 YDDDYYRKR 161
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
29-85 1.14e-06

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 48.96  E-value: 1.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  29 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFG--------------------LAKEYIDPETK 85
Cdd:cd06617   108 IAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ-----VKLCDFGisgylvdsvaktidagckpyMAPERINPELN 180
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-104 1.18e-06

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: 48.87  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKHipyrehkSLTG 98
Cdd:cd08228   101 RLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLGRFFSSKTTAAH-------SLVG 168

                  ....*.
gi 1398130438  99 TARYMS 104
Cdd:cd08228   169 TPYYMS 174
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
32-204 1.32e-06

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: 48.78  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLA-KEYIDPETKkhipyrehKSLTGTARYMSINTHLG 110
Cdd:cd14187   115 QIILGCQYLHRNRVIHRDLKLGNLFL----NDDMEV-KIGDFGLAtKVEYDGERK--------KTLCGTPNYIAPEVLSK 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 111 KEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATPIEVlcenFPEMATYLRYVRRLDFFEKPDYDy 190
Cdd:cd14187   182 KGHSFEVDIWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIPKHI----NPVAASLIQKMLQTDPTARPTIN- 253
                         170
                  ....*....|....
gi 1398130438 191 lrKLFTDLFDRKGY 204
Cdd:cd14187   254 --ELLNDEFFTSGY 265
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
32-76 1.51e-06

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: 48.53  E-value: 1.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:cd14078   109 QIVSAVAYVHSQGYAHRDLKPENLLLDEDQN-----LKLIDFGLC 148
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
32-86 1.57e-06

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: 48.37  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYIDPETKK 86
Cdd:cd14019   109 NLFKALKHVHSFGIIHRDVKPGNFLY----NRETGKGVLVDFGLAQREEDRPEQR 159
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-77 1.62e-06

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: 48.84  E-value: 1.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLELL--GPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAK 77
Cdd:cd14092    76 LVMELLrgGELLERIRKK--KRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDA--EIKIVDFGFAR 150
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
21-136 1.62e-06

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: 48.59  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyrehkSLTGT 99
Cdd:cd06620   101 FPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQ-----IKLCDFGVSGELINSIAD---------TFVGT 166
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1398130438 100 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06620   167 STYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
32-187 1.79e-06

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: 48.66  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPEN-FLIGrpgnkTQQVIHIIDFGLA-----KEYIDPETKKHIPYREHKSLTGTARYMSI 105
Cdd:cd14049   128 QLLEGVTYIHSMGIVHRDLKPRNiFLHG-----SDIHVRIGDFGLAcpdilQDGNDSTTMSRLNGLTHTSGVGTCLYAAP 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 106 NTHLGKEQSRRDDLEALGHMFMYFLRgslPWqglkaDTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEK 185
Cdd:cd14049   203 EQLEGSHYDFKSDMYSIGVILLELFQ---PF-----GTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSER 274

                  ..
gi 1398130438 186 PD 187
Cdd:cd14049   275 PS 276
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
13-150 1.83e-06

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: 48.81  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  13 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyidpetkkhIPYRE 92
Cdd:cd05632    93 IYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGH-----IRISDLGLAVK---------IPEGE 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  93 H-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 150
Cdd:cd05632   159 SiRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDR 217
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
1-148 1.97e-06

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: 48.57  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 79
Cdd:cd06654    94 VVMEYLaGGSLTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS-----VKLTDFGFCAQ- 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  80 IDPETKKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 148
Cdd:cd06654   166 ITPEQSK------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRALY 226
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
32-183 2.18e-06

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: 48.08  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGK 111
Cdd:cd14188   109 QIVSGLKYLHEQEILHRDLKLGNFFI----NENME-LKVGDFGLAARLEPLEHRR-------RTICGTPNYLSPEVLNKQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATP----------IEVLCENFPEMATYLRYVRRLD 181
Cdd:cd14188   177 GHGCESDIWALGCVMYTMLLGRPPFE---TTNLKETYRCIREARYSLPssllapakhlIASMLSKNPEDRPSLDEIIRHD 253

                  ..
gi 1398130438 182 FF 183
Cdd:cd14188   254 FF 255
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
13-158 2.30e-06

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: 48.36  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  13 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyidpetkkhipYRE 92
Cdd:cd05607    93 IYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGN-----CRLSDLGLAVE-----------VKE 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  93 HKSLT---GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKEryqkigDTKRAT 158
Cdd:cd05607   157 GKPITqraGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKE------ELKRRT 219
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
1-77 2.39e-06

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: 48.19  E-value: 2.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 77
Cdd:cd07846    77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSG-----VVKLCDFGFAR 148
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
35-107 2.40e-06

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: 48.21  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  35 SRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIH-IIDFGLAKE---------------YIDPETKKHIPYrehkslTG 98
Cdd:cd13989   113 SAISYLHENRIIHRDLKPENIVLQQGGGR---VIYkLIDLGYAKEldqgslctsfvgtlqYLAPELFESKKY------TC 183

                  ....*....
gi 1398130438  99 TARYMSINT 107
Cdd:cd13989   184 TVDYWSFGT 192
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
32-90 2.47e-06

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: 48.06  E-value: 2.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE--------------------YIDPETKKHIPY 90
Cdd:cd14162   108 QLVAGVEYCHSKGVVHRDLKCENLLLDKNNN-----LKITDFGFARGvmktkdgkpklsetycgsyaYASPEILRGIPY 181
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
37-153 2.65e-06

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: 48.17  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  37 MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK------------EYIDPETKKHIpyreHKSLTGTARYMS 104
Cdd:cd05609   113 LEYLHSYGIVHRDLKPDNLLITSMGH-----IKLTDFGLSKiglmslttnlyeGHIEKDTREFL----DKQVCGTPEYIA 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438 105 INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERY-QKIGD 153
Cdd:cd05609   184 PEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEELFgQVISD 230
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
2-123 2.84e-06

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: 47.90  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   2 VLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVihIIDFGLAKEYI 80
Cdd:cd14156    66 ILEYVsGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAV--VTDFGLAREVG 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  81 -----DPETKkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALG 123
Cdd:cd14156   144 empanDPERK--------LSLVGSAFWMAPEMLRGEPYDRKVDVFSFG 183
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
29-78 3.08e-06

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: 47.61  E-value: 3.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKE 78
Cdd:cd14000   117 IALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAIIIKIADYGISRQ 166
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
12-136 3.26e-06

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: 47.66  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeYIDPETKkhip 89
Cdd:cd14181   102 ELFDyLTEKvTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL-----DDQLHIKLSDFGFSC-HLEPGEK---- 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  90 YREhksLTGTARYMSI--------NTH--LGKEQsrrdDLEALGHMFMYFLRGSLPW 136
Cdd:cd14181   172 LRE---LCGTPGYLAPeilkcsmdETHpgYGKEV----DLWACGVILFTLLAGSPPF 221
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1-79 4.05e-06

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: 47.65  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14199   104 MVFELVkqGPVMEVP---TLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGH-----IKIADFGVSNE 175

                  .
gi 1398130438  79 Y 79
Cdd:cd14199   176 F 176
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
1-102 4.12e-06

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: 47.50  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07860    76 LVFEFLHQDLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA-----IKLADFGLARAF 150
                          90       100
                  ....*....|....*....|....*...
gi 1398130438  80 IDP-ETKKH----IPYREHKSLTGTARY 102
Cdd:cd07860   151 GVPvRTYTHevvtLWYRAPEILLGCKYY 178
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
32-136 4.20e-06

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: 47.12  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqviHIIDFGLAkEYIDPE-------TKKHIPyrehksltGTARYMS 104
Cdd:cd13991   106 QALEGLEYLHSRKILHGDVKADNVLLSSDGSDA----FLCDFGHA-ECLDPDglgkslfTGDYIP--------GTETHMA 172
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1398130438 105 INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd13991   173 PEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
29-159 4.27e-06

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: 47.69  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLIsrmeYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKkhipyrehKSLTGTARYMSINT 107
Cdd:cd05616   110 IAIGLF----FLQSKGIIYRDLKLDNVMLDSEGH-----IKIADFGMCKENIwDGVTT--------KTFCGTPDYIAPEI 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438 108 HLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkerYQKIGDTKRATP 159
Cdd:cd05616   173 IAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDEL---FQSIMEHNVAYP 221
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
1-151 4.33e-06

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: 47.10  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRTFSLKTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIHIIDFGLAKE 78
Cdd:cd14105    85 LILELV--AGGELFDFLAEKESLSEEEATEFlkQILDGVNYLHTKNIAHFDLKPENIML-LDKNVPIPRIKLIDFGLAHK 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  79 yIDPETkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd14105   162 -IEDGN-------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLG---DTKQETLANI 223
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1-155 4.71e-06

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: 47.33  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKE 78
Cdd:cd14175    72 LVTELMrGGELLDKI-LRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNP--ESLRICDFGFAKQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 yidpetkkhipYREHKSLTGTARYMS--INTHLGKEQSRRD--DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDT 154
Cdd:cd14175   149 -----------LRAENGLLMTPCYTAnfVAPEVLKRQGYDEgcDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSG 217

                  .
gi 1398130438 155 K 155
Cdd:cd14175   218 K 218
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
1-195 4.76e-06

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: 47.35  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDlCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyI 80
Cdd:cd07878    97 LVTNLMGADLNNIVK-CQK-LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE-----LRILDFGLARQ-A 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSINTHLgkeqsrrdDLEALGHMFMYFLRGSLPWQGLK-ADTLKERYQKIGdtkraTP 159
Cdd:cd07878   169 DDEMTGYVATRWYRAPEIMLNWMHYNQTV--------DIWSVGCIMAELLKGKALFPGNDyIDQLKRIMEVVG-----TP 235
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1398130438 160 I-EVLCENFPEMATylRYVRRLDFFEKPDydyLRKLF 195
Cdd:cd07878   236 SpEVLKKISSEHAR--KYIQSLPHMPQQD---LKKIF 267
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
14-86 4.85e-06

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: 47.36  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  14 FDLCDR-----------TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDP 82
Cdd:cd07865    98 FEFCEHdlagllsnknvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG-----VLKLADFGLARAFSLA 172

                  ....
gi 1398130438  83 ETKK 86
Cdd:cd07865   173 KNSQ 176
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1-80 4.93e-06

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: 47.27  E-value: 4.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnkTQQVIHIIDFGLAK--- 77
Cdd:cd07831    77 LVFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI------KDDILKLADFGSCRgiy 150

                  ....*....
gi 1398130438  78 ------EYI 80
Cdd:cd07831   151 skppytEYI 159
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
2-76 4.98e-06

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 47.24  E-value: 4.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438   2 VLELLGPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQvIHIIDFGLA 76
Cdd:cd14212    80 VFELLGVNLYELLKQNQfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN--LDSPE-IKLIDFGSA 152
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
32-137 4.98e-06

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: 47.17  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidpetkKHIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd14117   114 ELADALHYCHEKKVIHRDIKPENLLMGYKGE-----LKIADFGWS---------VHAPSLRRRTMCGTLDYLPPEMIEGR 179
                          90       100
                  ....*....|....*....|....*.
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14117   180 THDEKVDLWCIGVLCYELLVGMPPFE 205
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
19-76 5.01e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.58  E-value: 5.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:PHA03211  255 RPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPED-----ICLGDFGAA 307
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-90 5.01e-06

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: 46.98  E-value: 5.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKE--------------YIDPETKKHIPY 90
Cdd:cd14083   109 QVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSK--IMISDFGLSKMedsgvmstacgtpgYVAPEVLAQKPY 179
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
26-140 5.06e-06

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: 47.38  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  26 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYREHKSLTGTARYMSI 105
Cdd:cd07869   105 VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE-----LKLADFGLAR-------AKSVPSHTYSNEVVTLWYRPP 172
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1398130438 106 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLK 140
Cdd:cd07869   173 DVLLGStEYSTCLDMWGVGCIFVEMIQGVAAFPGMK 208
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
30-170 5.11e-06

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: 46.95  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNL---IYRDVKPENFLIGRPG---NKTQQVIHIIDFGLAKEYidpetkkhipyreHK----SLTGT 99
Cdd:cd14147   107 AVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIendDMEHKTLKITDFGLAREW-------------HKttqmSAAGT 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438 100 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC-ENFPEM 170
Cdd:cd14147   174 YAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGI--DCLAVAY-GVAVNKLTLPIPSTCpEPFAQL 242
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
3-111 5.12e-06

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: 46.92  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   3 LELLGPSLEDLFDLCDRTfSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyIDP 82
Cdd:cd14050    80 TELCDTSLQQYCEETHSL-PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG-----VCKLGDFGLVVE-LDK 152
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1398130438  83 ETKKHIpyrehksLTGTARYMS---INTHLGK 111
Cdd:cd14050   153 EDIHDA-------QEGDPRYMApelLQGSFTK 177
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
1-137 5.15e-06

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: 46.97  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14118    93 MVFELVdkGAVMEVP---TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH-----VKIADFGVSNE 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  79 Y--IDPETkkhipyrehKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14118   165 FegDDALL---------SSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFE 219
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-140 5.25e-06

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: 47.17  E-value: 5.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLFDlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKE 78
Cdd:cd14180    78 LVMELLrgGELLDRIKK--KARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGA--VLKVIDFGFARL 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  79 YIDPETKKHIPyrehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 140
Cdd:cd14180   154 RPQGSRPLQTP-------CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKR 208
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
32-151 5.44e-06

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: 47.18  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd05585   102 ELLCALECLHKFNVIYRDLKPENILLDYTGH-----IALCDFGLCKLNMKDDDKTN-------TFCGTPEYLAPELLLGH 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd05585   170 GYTKAVDWWTLGVLLYEMLTGLPPFYD---ENTNEMYRKI 206
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
32-104 5.90e-06

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: 46.63  E-value: 5.90e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAkeyidpetkKHIPYREH-KSLTGTARYMS 104
Cdd:cd06632   110 QILSGLAYLHSRNTVHRDIKGANILVDTNG-----VVKLADFGMA---------KHVEAFSFaKSFKGSPYWMA 169
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
29-136 6.40e-06

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: 46.80  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehksltGTARYMSINTH 108
Cdd:cd06619   100 IAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ-----VKLCDFGVSTQLVNSIAKTYV---------GTNAYMAPERI 165
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 109 LGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06619   166 SGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
18-104 7.26e-06

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: 46.50  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKeYIDPETKkhipyrEHKSLT 97
Cdd:cd08224    98 KRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG-----VVKLGDLGLGR-FFSSKTT------AAHSLV 165

                  ....*..
gi 1398130438  98 GTARYMS 104
Cdd:cd08224   166 GTPYYMS 172
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
11-203 7.44e-06

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: 46.71  E-value: 7.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  11 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPETKKhip 89
Cdd:cd05054   125 EDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPDYVR--- 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  90 yrehkslTGTAR----YMSINTHLGKEQSRRDDLEALGhMFMY--FLRGSLPWQGLKADtlKERYQKIGDTKRATPievl 163
Cdd:cd05054   197 -------KGDARlplkWMAPESIFDKVYTTQSDVWSFG-VLLWeiFSLGASPYPGVQMD--EEFCRRLKEGTRMRA---- 262
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1398130438 164 cenfPEMATYLRYVRRLDFFEKPDYDylRKLFTDLFDRKG 203
Cdd:cd05054   263 ----PEYTTPEIYQIMLDCWHGEPKE--RPTFSELVEKLG 296
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
1-148 7.92e-06

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: 46.64  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 79
Cdd:cd06656    93 VVMEYLaGGSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-----VKLTDFGFCAQ- 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  80 IDPETKKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 148
Cdd:cd06656   165 ITPEQSK------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALY 225
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
32-102 8.21e-06

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: 46.40  E-value: 8.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE----TKKHIP--YREHKSLTGTARY 102
Cdd:cd07840   112 QLLEGLQYLHSNGILHRDIKGSNILINNDGV-----LKLADFGLARPYTKENnadyTNRVITlwYRPPELLLGATRY 183
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
32-136 8.29e-06

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: 46.19  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehKSLTGTARYMSINTHLGK 111
Cdd:cd06625   110 QILEGLAYLHSNMIVHRDIKGANILRDSNGN-----VKLGDFGASKRLQTICSSTGM-----KSVTGTPYWMSPEVINGE 179
                          90       100
                  ....*....|....*....|....*
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06625   180 GYGRKADIWSVGCTVVEMLTTKPPW 204
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
1-76 8.47e-06

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: 46.18  E-value: 8.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438   1 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLA 76
Cdd:cd14184    76 LVMELVKGG--DLFDAITSStkYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKS-LKLGDFGLA 150
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
32-136 8.65e-06

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: 46.25  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKeyIDPETKkhipYRehKSLTGTARYMSINTHLGK 111
Cdd:cd14082   111 QILVALRYLHSKNIVHCDLKPENVLLASAEPFPQ--VKLCDFGFAR--IIGEKS----FR--RSVVGTPAYLAPEVLRNK 180
                          90       100
                  ....*....|....*....|....*
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd14082   181 GYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1-123 8.85e-06

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: 46.17  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKN--LIYRDVKPENFLIGRPGNktqqvIHIIDFGLA- 76
Cdd:cd13985    79 LLMEYCPGSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR-----FKLCDFGSAt 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  77 KEYIDPETKKHIPYRE-----HKSLTGTARYMsINTHLGKEQSRRDDLEALG 123
Cdd:cd13985   154 TEHYPLERAEEVNIIEeeiqkNTTPMYRAPEM-IDLYSKKPIGEKADIWALG 204
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
21-141 9.06e-06

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: 46.28  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTKKhipyREHKSLtGTA 100
Cdd:cd05606    95 FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGH-----VRISDLGLACDF----SKK----KPHASV-GTH 160
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 101 RYMSINTHL-GKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 141
Cdd:cd05606   161 GYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKT 202
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
12-76 9.82e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 46.76  E-value: 9.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  12 DLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvihIIDFGLA 76
Cdd:PHA03207  171 DLFTYVDRSgpLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAV-----LGDFGAA 232
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
32-104 9.98e-06

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: 46.66  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYiDPETKKHIP-------YREHKSLTGTARYMS 104
Cdd:cd07853   111 QILRGLKYLHSAGILHRDIKPGNLLV-----NSNCVLKICDFGLARVE-EPDESKHMTqevvtqyYRAPEILMGSRHYTS 184
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
32-77 1.01e-05

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: 46.13  E-value: 1.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 77
Cdd:cd07835   107 QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA-----LKLADFGLAR 147
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
1-144 1.07e-05

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: 46.10  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHI--IDFGLA 76
Cdd:cd14196    85 LILELV--SGGELFDFLAQKESLseEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML---LDKNIPIPHIklIDFGLA 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  77 KEYIDPEtkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 144
Cdd:cd14196   160 HEIEDGV--------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
32-78 1.13e-05

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: 46.21  E-value: 1.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14046   112 QILEGLAYIHSQGIIHRDLKPVNIFLDSNGN-----VKIGDFGLATS 153
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1-82 1.19e-05

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: 46.21  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 80
Cdd:cd07845    85 LVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG-----CLKIADFGLARTYG 159

                  ..
gi 1398130438  81 DP 82
Cdd:cd07845   160 LP 161
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-104 1.21e-05

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: 46.18  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKHipyrehkSLTG 98
Cdd:cd08229   123 RLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLGRFFSSKTTAAH-------SLVG 190

                  ....*.
gi 1398130438  99 TARYMS 104
Cdd:cd08229   191 TPYYMS 196
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
11-203 1.23e-05

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: 46.15  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  11 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPETKKhip 89
Cdd:cd14207   167 EDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKNPDYVR--- 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  90 yrehkslTGTAR----YMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKAD-----TLKEryqkiGDTKRAtp 159
Cdd:cd14207   239 -------KGDARlplkWMAPESIFDKIYSTKSDVWSYGvLLWEIFSLGASPYPGVQIDedfcsKLKE-----GIRMRA-- 304
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1398130438 160 ievlcenfPEMATYLRYVRRLDFFEKPDYDylRKLFTDLFDRKG 203
Cdd:cd14207   305 --------PEFATSEIYQIMLDCWQGDPNE--RPRFSELVERLG 338
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-107 1.38e-05

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: 45.72  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  26 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNktQQVIH-IIDFGLAKE---------------YIDPEtkkhip 89
Cdd:cd14038   103 ILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGE--QRLIHkIIDLGYAKEldqgslctsfvgtlqYLAPE------ 173
                          90
                  ....*....|....*...
gi 1398130438  90 YREHKSLTGTARYMSINT 107
Cdd:cd14038   174 LLEQQKYTVTVDYWSFGT 191
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
30-170 1.38e-05

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: 45.80  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKN---LIYRDVKPENFLIGRP------GNKTqqvIHIIDFGLAKEYidpetkkhipYREHK-SLTGT 99
Cdd:cd14146   108 AVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddiCNKT---LKITDFGLAREW----------HRTTKmSAAGT 174
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438 100 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC-ENFPEM 170
Cdd:cd14146   175 YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI--DGLAVAY-GVAVNKLTLPIPSTCpEPFAKL 243
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
32-160 1.39e-05

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: 45.84  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEyidpetKKHIpYREHK--SLTGTARYMS---IN 106
Cdd:cd06629   116 QILDGLAYLHSKGILHRDLKADNILV-----DLEGICKISDFGISKK------SDDI-YGNNGatSMQGSVFWMApevIH 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438 107 ThLGKEQSRRDDLEALGHMFMYFLRGSLPWqglkadTLKERYQ---KIGDTKRATPI 160
Cdd:cd06629   184 S-QGQGYSAKVDIWSLGCVVLEMLAGRRPW------SDDEAIAamfKLGNKRSAPPV 233
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
12-79 1.39e-05

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: 45.72  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  12 DLFD-LCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgNKTQQVIHIIDFGLAKEY 79
Cdd:cd14192    87 ELFDrITDESYQLTEldAILFTRQICEGVHYLHQHYILHLDLKPENILCV---NSTGNQIKIIDFGLARRY 154
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
32-75 1.42e-05

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: 45.72  E-value: 1.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 75
Cdd:cd14079   110 QIISGVEYCHRHMVVHRDLKPENLLLDSNMN-----VKIADFGL 148
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1-78 1.47e-05

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: 45.57  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDL---FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAK 77
Cdd:cd14137    80 LVMEYMPETLYRVirhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV----DPETGVLKLCDFGSAK 155

                  .
gi 1398130438  78 E 78
Cdd:cd14137   156 R 156
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1-90 1.53e-05

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: 45.53  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQVIHIIDFGLAKE 78
Cdd:cd14171    86 IVMELMEGG--ELFDRIsqHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKD--NSEDAPIKLCDFGFAKV 161
                          90
                  ....*....|...
gi 1398130438  79 YI-DPETKKHIPY 90
Cdd:cd14171   162 DQgDLMTPQFTPY 174
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
1-123 1.59e-05

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: 45.46  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLeDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKe 78
Cdd:cd14004    85 LVMEKHGSGM-DLFDFIERKPNMdeKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT-----IKLIDFGSAA- 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 YIDPEtkkhiPYrehKSLTGTARYMSI-----NTHLGKEQsrrdDLEALG 123
Cdd:cd14004   158 YIKSG-----PF---DTFVGTIDYAAPevlrgNPYGGKEQ----DIWALG 195
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
7-76 1.72e-05

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: 45.46  E-value: 1.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPEN-FLigrpgnKTQQVIHIIDFGLA 76
Cdd:cd14062    72 GSSLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNiFL------HEDLTVKIGDFGLA 136
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
39-137 1.73e-05

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: 45.28  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  39 YVHSKNLIYRDVKPENFLI--GRpgnktqqvIHIIDFGLAKEyIDPETkKHIpYREHKSltGTARYMS------INTHLG 110
Cdd:cd14131   118 TIHEEGIVHSDLKPANFLLvkGR--------LKLIDFGIAKA-IQNDT-TSI-VRDSQV--GTLNYMSpeaikdTSASGE 184
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1398130438 111 KEQ----SRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14131   185 GKPkskiGRPSDVWSLGCILYQMVYGKTPFQ 215
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
21-104 1.87e-05

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: 45.42  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyrehKSLTGTA 100
Cdd:cd05605    99 FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH-----VRISDLGLAVEIPEGETI--------RGRVGTV 165

                  ....
gi 1398130438 101 RYMS 104
Cdd:cd05605   166 GYMA 169
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
21-137 1.91e-05

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: 45.82  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqviHIIDFGLAKEYidpeTKKhipyREHKSLtGTA 100
Cdd:cd05633   105 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV-----RISDLGLACDF----SKK----KPHASV-GTH 170
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1398130438 101 RYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd05633   171 GYMAPEVlQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
1-155 1.99e-05

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: 45.40  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKE 78
Cdd:cd14176    90 VVTELMkGGELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNP--ESIRICDFGFAKQ 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 yidpetkkhipYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIG 152
Cdd:cd14176   167 -----------LRAENGLLMTPCYTA--NFVAPEVLERQgydaacDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIG 233

                  ...
gi 1398130438 153 DTK 155
Cdd:cd14176   234 SGK 236
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
12-138 2.03e-05

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: 45.30  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFD-LCDRTFSLKTV--LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgNKTQQVIHIIDFGLAKEYiDPETKKHI 88
Cdd:cd14190    87 ELFErIVDEDYHLTEVdaMVFVRQICEGIQFMHQMRVLHLDLKPENILCV---NRTGHQVKIIDFGLARRY-NPREKLKV 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  89 PYrehksltGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14190   163 NF-------GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLG 205
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
30-198 2.05e-05

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: 44.98  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKN---LIYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYidPETKKhipyrehKSLTGTARYM 103
Cdd:cd14148    98 AVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienDDLSGKTLKITDFGLAREW--HKTTK-------MSAAGTYAWM 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 104 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDTKRATPIEVLCenfPE-MATYLRYVRRLDF 182
Cdd:cd14148   169 APEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR--EIDALAVAY-GVAMNKLTLPIPSTC---PEpFARLLEECWDPDP 242
                         170
                  ....*....|....*.
gi 1398130438 183 FEKPDYDYLRKLFTDL 198
Cdd:cd14148   243 HGRPDFGSILKRLEDI 258
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
30-164 2.09e-05

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: 45.08  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKN---LIYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYidpetkkhipYREHK-SLTGTARY 102
Cdd:cd14061    98 AIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienEDLENKTLKITDFGLAREW----------HKTTRmSAAGTYAW 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438 103 MS---INTHLgkeQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC 164
Cdd:cd14061   168 MApevIKSST---FSKASDVWSYGVLLWELLTGEVPYKGI--DGLAVAY-GVAVNKLTLPIPSTC 226
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
12-135 2.30e-05

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: 45.17  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKeyidPETKKhipyr 91
Cdd:cd13975    90 DLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDK-----KNRAKITDLGFCK----PEAMM----- 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  92 eHKSLTGTARYMSINTHLGKEQSRRdDLEALGHMFMYFLRGS--LP 135
Cdd:cd13975   156 -SGSIVGTPIHMAPELFSGKYDNSV-DVYAFGILFWYLCAGHvkLP 199
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
27-137 2.31e-05

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: 45.17  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  27 LMIAIQLISRMEYVHSKNLIYRDVKPENFL--IGRPGnktQQVIHIIDFGLAKEYIDPEtkkhipyrEHKSLTGTARYMS 104
Cdd:cd13988    99 LIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDG---QSVYKLTDFGAARELEDDE--------QFVSLYGTEEYLH 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398130438 105 --------INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd13988   168 pdmyeravLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
1-78 2.39e-05

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: 44.93  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GpslEDLFD--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNkTQQVIHIIDFGLAK 77
Cdd:cd14091    71 LVTELLrG---GELLDriLRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESG-DPESLRICDFGFAK 146

                  .
gi 1398130438  78 E 78
Cdd:cd14091   147 Q 147
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-90 2.39e-05

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: 45.11  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQ-QVIHIIDFGLAKE----------------YIDPETKKHIPY 90
Cdd:cd14086   108 QILESVNHCHQNGIVHRDLKPENLLL---ASKSKgAAVKLADFGLAIEvqgdqqawfgfagtpgYLSPEVLRKDPY 180
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
32-147 2.46e-05

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: 44.69  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyrehKSLTGTARYMSINTHLGK 111
Cdd:cd14071   107 QILSAVEYCHKRHIVHRDLKAENLLLDANMN-----IKIADFGFSNFFKPGELL--------KTWCGSPPYAAPEVFEGK 173
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1398130438 112 EQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 147
Cdd:cd14071   174 EYEGPQlDIWSLGVVLYVLVCGALPFDGSTLQTLRDR 210
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
19-77 2.54e-05

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: 44.97  E-value: 2.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:cd05034    87 RALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGE-----NNVCKVADFGLAR 140
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1-77 2.71e-05

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: 45.06  E-value: 2.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 77
Cdd:cd07844    75 LVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE-----LKLADFGLAR 146
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1-144 2.76e-05

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: 45.01  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPEN-FLIGRpgNKTQQVIHIIDFGLAK 77
Cdd:cd14194    85 LILELVAGG--ELFDFLAEKESLteEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDR--NVPKPRIKIIDFGLAH 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  78 EyIDPETkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 144
Cdd:cd14194   161 K-IDFGN-------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-135 3.17e-05

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: 44.60  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKTQQVIHIIDFGLAKEYIDP---ETKKHIPYREHK 94
Cdd:cd14172    97 DQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLY--TSKEKDAVLKLTDFGFAKETTVQnalQTPCYTPYYVAP 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398130438  95 SLTGTARYmsinthlgkeqSRRDDLEALGhMFMYFLRGSLP 135
Cdd:cd14172   175 EVLGPEKY-----------DKSCDMWSLG-VIMYILLCGFP 203
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
12-79 3.43e-05

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: 44.52  E-value: 3.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  12 DLFD-LCDRTFSLK---TVLMIAiQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqqvIHIIDFGLAKEY 79
Cdd:cd14193    87 ELFDrIIDENYNLTeldTILFIK-QICEGIQYMHQMYILHLDLKPENILcVSREANQ----VKIIDFGLARRY 154
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
32-163 3.89e-05

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: 44.48  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidPETKKHipyREHKSLTGTARYMSINTHLG- 110
Cdd:cd05586   104 ELVLALEHLHKNDIVYRDLKPENILLDANGH-----IALCDFGLSK----ADLTDN---KTTNTFCGTTEYLAPEVLLDe 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1398130438 111 KEQSRRDDLEALGHMFMYFLRGslpWQGLKADTLKERYQKIGDTKRATPIEVL 163
Cdd:cd05586   172 KGYTKMVDFWSLGVLVFEMCCG---WSPFYAEDTQQMYRNIAFGKVRFPKDVL 221
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
32-79 4.13e-05

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: 44.45  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEY 79
Cdd:cd14132   120 ELLKALDYCHSKGIMHRDVKPHNIMI----DHEKRKLRLIDWGLAEFY 163
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
13-171 4.15e-05

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: 44.21  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  13 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyre 92
Cdd:cd05631    91 IYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH-----IRISDLGLAVQIPEGETV------- 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  93 hKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYqkigDTKRATPIEVLCENFPEMA 171
Cdd:cd05631   159 -RGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEV----DRRVKEDQEEYSEKFSEDA 232
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
9-103 4.18e-05

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: 44.37  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   9 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVH--SKNLIYRDVKPENFLIgrpgNKTQQVIhIIDFGLAKEYIdpETKK 86
Cdd:cd13978    78 SLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL----DNHFHVK-ISDFGLSKLGM--KSIS 150
                          90
                  ....*....|....*..
gi 1398130438  87 HIPYREHKSLTGTARYM 103
Cdd:cd13978   151 ANRRRGTENLGGTPIYM 167
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
1-150 4.19e-05

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: 44.08  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRP--GNKTQQVIHIIDFGLAK 77
Cdd:cd14097    77 LVMELCeDGELKELLLR-KGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiiDNNDKLNIKVTDFGLSV 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  78 EyidpetKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 150
Cdd:cd14097   156 Q------KYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK 222
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
21-102 4.23e-05

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: 44.41  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA----KEYIDPETKKHIP--YREHK 94
Cdd:cd07864   113 FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ-----IKLADFGLArlynSEESRPYTNKVITlwYRPPE 187

                  ....*...
gi 1398130438  95 SLTGTARY 102
Cdd:cd07864   188 LLLGEERY 195
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-102 4.26e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 44.42  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqVIHIIDFGLAKEY 79
Cdd:PLN00009   78 LVFEYLDLDLKKHMDSSpDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN----ALKLADFGLARAF 153
                          90       100
                  ....*....|....*....|....*...
gi 1398130438  80 -IDPETKKH----IPYREHKSLTGTARY 102
Cdd:PLN00009  154 gIPVRTFTHevvtLWYRAPEILLGSRHY 181
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
37-103 4.38e-05

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: 44.27  E-value: 4.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  37 MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyREHKSLTGTARYM 103
Cdd:cd06610   115 LEYLHSNGQIHRDVKAGNILLGEDGS-----VKIADFGVSASLATGGDRTR---KVRKTFVGTPCWM 173
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-135 4.59e-05

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: 44.28  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKN-LIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 107
Cdd:cd06650   108 VSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 173
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 108 HLGKEQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:cd06650   174 LQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
1-89 4.84e-05

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: 43.97  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE- 78
Cdd:cd05041    70 IVMELVpGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENN-----VLKISDFGMSREe 144
                          90
                  ....*....|....*
gi 1398130438  79 ----YIDPETKKHIP 89
Cdd:cd05041   145 edgeYTVSDGLKQIP 159
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
32-138 4.96e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 44.62  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPetkkhIPYREHKSLTGTARYMSINTHLGK 111
Cdd:PTZ00267  177 QIVLALDEVHSRKMMHRDLKSANIFLMPTG-----IIKLGDFGFSKQYSDS-----VSLDVASSFCGTPYYLAPELWERK 246
                          90       100
                  ....*....|....*....|....*..
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:PTZ00267  247 RYSKKADMWSLGVILYELLTLHRPFKG 273
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
1-57 4.98e-05

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: 44.10  E-value: 4.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLELLGPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLI 57
Cdd:cd14136    95 MVFEVLGPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLL 153
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
30-136 5.22e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 44.20  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYidpETKKHipyrehkSLTGTARYMSINTHL 109
Cdd:PTZ00426  137 AAQIVLIFEYLQSLNIVYRDLKPENLLLDKDG-----FIKMTDFGFAKVV---DTRTY-------TLCGTPEYIAPEILL 201
                          90       100
                  ....*....|....*....|....*..
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:PTZ00426  202 NVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
1-106 5.25e-05

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: 44.26  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDlCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYI 80
Cdd:cd07877    99 LVTHLMGADLNNIVK-CQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE-----LKILDFGLAR-HT 170
                          90       100
                  ....*....|....*....|....*.
gi 1398130438  81 DPETKKHIPYREHKSLTGTARYMSIN 106
Cdd:cd07877   171 DDEMTGYVATRWYRAPEIMLNWMHYN 196
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
32-79 5.49e-05

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: 44.01  E-value: 5.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd14076   114 QLISGVAYLHKKGVVHRDLKLENLLLDKNRN-----LVITDFGFANTF 156
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
22-92 5.51e-05

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: 44.12  E-value: 5.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYidPETKKHIPYRE 92
Cdd:cd05080   105 GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN-----DRLVKIGDFGLAKAV--PEGHEYYRVRE 168
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
32-83 5.54e-05

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: 43.71  E-value: 5.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE 83
Cdd:cd14080   110 QLALAVQYLHSLDIAHRDLKCENILLDSNNN-----VKLSDFGFARLCPDDD 156
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
29-76 5.60e-05

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: 44.09  E-value: 5.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLA 76
Cdd:cd07852   112 IMYQLLKALKYLHSGGVIHRDLKPSNILL-----NSDCRVKLADFGLA 154
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
35-107 5.67e-05

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: 44.14  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  35 SRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvIH-IIDFGLAK---------------EYIDPEtkkhipYREHKSLTG 98
Cdd:cd14039   110 SGIQYLHENKIIHRDLKPENIVLQEINGKI---VHkIIDLGYAKdldqgslctsfvgtlQYLAPE------LFENKSYTV 180

                  ....*....
gi 1398130438  99 TARYMSINT 107
Cdd:cd14039   181 TVDYWSFGT 189
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-92 6.16e-05

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: 43.65  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRT---FSLKTVLMIAIQLISRMEYVH-SKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGL 75
Cdd:cd08528    86 IVMELIeGAPLGEHFSSLKEKnehFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLG-----EDDKVTITDFGL 160
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1398130438  76 AKE----------------YIDPETKKHIPYRE 92
Cdd:cd08528   161 AKQkgpesskmtsvvgtilYSCPEIVQNEPYGE 193
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
8-144 6.31e-05

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: 43.80  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   8 PSLEDLFD---LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-----EY 79
Cdd:cd05099   115 PGPDYTFDitkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLV-----TEDNVMKIADFGLARgvhdiDY 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  80 IDPETKKHIPYrehKSLTGTARYMSINTHlgkeQSRRDDLEALghMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05099   190 YKKTSNGRLPV---KWMAPEALFDRVYTH----QSDVWSFGIL--MWEIFTLGGSPYPGIPVEEL 245
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
17-87 6.82e-05

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: 43.89  E-value: 6.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  17 CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKKH 87
Cdd:cd07855   102 SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE-----LKIGDFGMARG-LCTSPEEH 166
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
32-87 6.98e-05

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: 43.67  E-value: 6.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAKEYIDPETKKH 87
Cdd:cd07834   111 QILRGLKYLHSAGVIHRDLKPSNILV----NSNCDL-KICDFGLARGVDPDEDKGF 161
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
21-137 7.01e-05

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: 43.88  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTKKhipyREHKSLtGTA 100
Cdd:cd14223   100 FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH-----VRISDLGLACDF----SKK----KPHASV-GTH 165
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1398130438 101 RYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14223   166 GYMAPEVlQKGVAYDSSADWFSLGCMLFKLLRGHSPFR 203
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
29-83 7.99e-05

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: 43.56  E-value: 7.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA--------------KEYIDPE 83
Cdd:cd14052   111 ILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT-----LKIGDFGMAtvwplirgieregdREYIAPE 174
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
29-160 8.20e-05

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: 43.15  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKeyidpETKKHIPYREhkslTGTARYMSINTH 108
Cdd:cd08530   108 IFIQMLRGLKALHDQKILHRDLKSANILLSAGD-----LVKIGDLGISK-----VLKKNLAKTQ----IGTPLYAAPEVW 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438 109 LGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKrATPI 160
Cdd:cd08530   174 KGRPYDYKSDIWSLGCLLYEMATFRPPFE---ARTMQELRYKVCRGK-FPPI 221
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1-102 8.20e-05

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: 43.48  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL--GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKTQQVIHIIDFGLAKE 78
Cdd:cd14170    76 IVMECLdgGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY--TSKRPNAILKLTDFGFAKE 153
                          90       100
                  ....*....|....*....|....*..
gi 1398130438  79 ---YIDPETKKHIPYREHKSLTGTARY 102
Cdd:cd14170   154 ttsHNSLTTPCYTPYYVAPEVLGPEKY 180
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
1-95 8.38e-05

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: 43.71  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYI 80
Cdd:cd07856    87 FVTELLGTDLHRL--LTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCD-----LKICDFGLAR-IQ 158
                          90
                  ....*....|....*
gi 1398130438  81 DPETKKHIPYREHKS 95
Cdd:cd07856   159 DPQMTGYVSTRYYRA 173
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
21-83 8.64e-05

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: 43.21  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPE 83
Cdd:cd05059    97 FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG-----EQNVVKVSDFGLARYVLDDE 154
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
32-79 8.76e-05

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: 43.41  E-value: 8.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07863   116 QFLRGLDFLHANCIVHRDLKPENILVTSGGQ-----VKLADFGLARIY 158
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
17-123 8.91e-05

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: 43.19  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  17 CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyIDPEtkkhipYREHKSL 96
Cdd:cd08221    94 KNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD-----LVKLGDFGISKV-LDSE------SSMAESI 161
                          90       100
                  ....*....|....*....|....*..
gi 1398130438  97 TGTARYMSINTHLGKEQSRRDDLEALG 123
Cdd:cd08221   162 VGTPYYMSPELVQGVKYNFKSDIWAVG 188
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
24-79 9.28e-05

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: 43.48  E-value: 9.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  24 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07862   110 ETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ-----IKLADFGLARIY 160
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
29-103 9.42e-05

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: 43.46  E-value: 9.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  29 IAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipYREHkSLTGTARYM 103
Cdd:cd05598   107 IA-ELVCAIESVHKMGFIHRDIKPDNILIDRDGH-----IKLTDFGLCTGFRWTHDSKY--YLAH-SLVGTPNYI 172
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
32-141 1.04e-04

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: 43.09  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYREH---KSLTGTARYMSINTH 108
Cdd:cd06653   114 QILQGVSYLHSNMIVHRDIKGANILRDSAGN-----VKLGDFGASK-------RIQTICMSGtgiKSVTGTPYWMSPEVI 181
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1398130438 109 LGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 141
Cdd:cd06653   182 SGEGYGRKADVWSVACTVVEMLTEKPPWAEYEA 214
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
5-123 1.04e-04

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: 43.23  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   5 LLGPSLEDLFDLCDRTfSLKTvLMIA-------IQLISR-----MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIID 72
Cdd:cd06917    72 LKGPSLWIIMDYCEGG-SIRT-LMRAgpiaeryIAVIMRevlvaLKFIHKDGIIHRDIKAANILVTNTGN-----VKLCD 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  73 FGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHL-GKEQSRRDDLEALG 123
Cdd:cd06917   145 FGVAASLNQNSSKR-------STFVGTPYWMAPEVITeGKYYDTKADIWSLG 189
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
8-144 1.07e-04

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: 43.47  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   8 PSLEDLFDLC---DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-----EY 79
Cdd:cd05100   115 PGMDYSFDTCklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV-----TEDNVMKIADFGLARdvhniDY 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  80 IDPETKKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05100   190 YKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLLWEIFTLGGSPYPGIPVEEL 245
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
29-144 1.07e-04

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: 43.15  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLIsrmeYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTH 108
Cdd:cd05587   106 IAVGLF----FLHSKGIIYRDLKLDNVMLDAEGH-----IKIADFGMCKEGIFGGKTT-------RTFCGTPDYIAPEII 169
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1398130438 109 LGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05587   170 AYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDEL 205
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
32-79 1.13e-04

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: 43.16  E-value: 1.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07857   113 QILCGLKYIHSANVLHRDLKPGNLLVNADCE-----LKICDFGLARGF 155
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
32-82 1.16e-04

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: 43.04  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtQQVIHIIDFGLAKEYIDP 82
Cdd:cd07842   116 QILNGIHYLHSNWVLHRDLKPANILVMGEGPE-RGVVKIGDLGLARLFNAP 165
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
7-139 1.19e-04

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: 43.13  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyidpETKK 86
Cdd:cd14151    87 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLTVKIGDFGLAT-----VKSR 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  87 HIPYREHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGL 139
Cdd:cd14151   157 WSGSHQFEQLSGSILWMApevIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI 212
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
32-147 1.20e-04

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: 42.81  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLI-------------GRPGNKTQQ---------------VIHIIDFGLAKEYIDPE 83
Cdd:cd14096   114 QVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrKADDDETKVdegefipgvggggigIVKLADFGLSKQVWDSN 193
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  84 TkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKER 147
Cdd:cd14096   194 T---------KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESIETLTEK 248
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
1-77 1.25e-04

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: 42.63  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438   1 MVLELLGP-SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAK 77
Cdd:cd14068    62 LVMELAPKgSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIAKIADYGIAQ 139
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1-138 1.31e-04

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: 42.63  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELlgPSLEDLFD-LCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd14161    79 IVMEY--ASRGDLYDyISERQrLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN-----IKIADFGLSNL 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  79 YidpETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14161   152 Y---NQDKFL-----QTYCGSPLYASPEIVNGRPYIGPEvDSWSLGVLLYILVHGTMPFDG 204
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
18-78 1.32e-04

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: 42.66  E-value: 1.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktQQVIHIIDFGLAKE 78
Cdd:cd14089    94 DSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGP--NAILKLTDFGFAKE 152
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
19-138 1.43e-04

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: 42.71  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYIDPETKKHIPYREHKSLTG 98
Cdd:cd14173    95 RHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSP--VKICDFDLGSGIKLNSDCSPISTPELLTPCG 172
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438  99 TARYMS--INTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14173   173 SAEYMApeVVEAFNEEASiydKRCDLWSLGVILYIMLSGYPPFVG 217
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
25-77 1.43e-04

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: 42.79  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  25 TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:cd05052   105 VLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGE-----NHLVKVADFGLSR 152
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
32-137 1.51e-04

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: 42.67  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLI-GRPGNKtqqvIHIIDFGLakeyidpeTKKHIPYREHKSLTGTARYMSINTHLG 110
Cdd:cd14665   104 QLISGVSYCHSMQICHRDLKLENTLLdGSPAPR----LKICDFGY--------SKSSVLHSQPKSTVGTPAYIAPEVLLK 171
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 111 KE-QSRRDDLEALGHMFMYFLRGSLPWQ 137
Cdd:cd14665   172 KEyDGKIADVWSCGVTLYVMLVGAYPFE 199
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
35-138 1.73e-04

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: 42.32  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  35 SRMEYVHSKNLIYRDVKPENFLIGRPgNKTQQViHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMS-----INTHL 109
Cdd:cd14174   111 SALDFLHTKGIAHRDLKPENILCESP-DKVSPV-KICDFDLGSGVKLNSACTPITTPELTTPCGSAEYMApevveVFTDE 188
                          90       100
                  ....*....|....*....|....*....
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14174   189 ATFYDKRCDLWSLGVILYIMLSGYPPFVG 217
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
1-76 1.80e-04

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: 42.29  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI--GRPGNKTqqvIHIIDFGLA 76
Cdd:cd14183    81 LVMELVKGG--DLFDAITSTnkYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKS---LKLGDFGLA 155
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
32-141 1.80e-04

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: 42.34  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTKKHIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd06652   114 QILEGVHYLHSNMIVHRDIKGANILRDSVGN-----VKLGDFGASKRL----QTICLSGTGMKSVTGTPYWMSPEVISGE 184
                          90       100       110
                  ....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKA 141
Cdd:cd06652   185 GYGRKADIWSVGCTVVEMLTEKPPWAEFEA 214
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-90 1.81e-04

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: 42.57  E-value: 1.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK--------------EYIDPETKKHIPY 90
Cdd:cd14169   109 QVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSK--IMISDFGLSKieaqgmlstacgtpGYVAPELLEQKPY 179
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
32-102 1.90e-04

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: 42.41  E-value: 1.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY-IDPETKKH----IPYREHKSLTGTARY 102
Cdd:cd07861   109 QILQGILFCHSRRVLHRDLKPQNLLIDNKG-----VIKLADFGLARAFgIPVRVYTHevvtLWYRAPEVLLGSPRY 179
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
19-172 1.92e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 42.93  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKhipyrEHKSLTG 98
Cdd:PTZ00283  138 RTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG-----LVKLGDFGFSKMYAATVSDD-----VGRTFCG 207
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  99 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-----TLKERYQKIGDTKRatpievlcenfPEMAT 172
Cdd:PTZ00283  208 TPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEevmhkTLAGRYDPLPPSIS-----------PEMQE 275
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1-82 1.98e-04

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: 42.18  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnkTQQVIHIIDFGLAKE 78
Cdd:cd14107    75 LILELC--SSEELLDRLFLKGVVteAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSP---TREDIKICDFGFAQE 149

                  ....
gi 1398130438  79 yIDP 82
Cdd:cd14107   150 -ITP 152
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
9-83 2.11e-04

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: 42.56  E-value: 2.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438   9 SLEDLFDLCDRTFSLKTVLMIAIQLisrmEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE 83
Cdd:cd05610    93 SLLHIYGYFDEEMAVKYISEVALAL----DYLHRHGIIHRDLKPDNMLISNEGH-----IKLTDFGLSKVTLNRE 158
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
21-137 2.15e-04

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: 41.86  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYIDPetkkhipyrEHKSLTGT- 99
Cdd:cd05112    97 FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGE-----NQVVKVSDFGMTRFVLDD---------QYTSSTGTk 162
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 100 --ARYMSINTHLGKEQSRRDDLEALGhMFMY--FLRGSLPWQ 137
Cdd:cd05112   163 fpVKWSSPEVFSFSRYSSKSDVWSFG-VLMWevFSEGKIPYE 203
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
12-136 2.16e-04

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: 42.21  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKKhip 89
Cdd:cd14182    96 ELFDyLTEKvTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN-----IKLTDFGFSCQ-LDPGEKL--- 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  90 yrehKSLTGTARYM-------SINTH---LGKEQsrrdDLEALGHMFMYFLRGSLPW 136
Cdd:cd14182   167 ----REVCGTPGYLapeiiecSMDDNhpgYGKEV----DMWSTGVIMYTLLAGSPPF 215
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
37-78 2.36e-04

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: 42.29  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1398130438  37 MEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 78
Cdd:cd05589   114 LQFLHEHKIVYRDLKLDNLLLDTEG-----YVKIADFGLCKE 150
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-74 2.37e-04

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 42.38  E-value: 2.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438   4 ELLGPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktQQVIHIIDFG 74
Cdd:cd14225   125 ELLGMNLYELIKKNNfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRG---QSSIKVIDFG 193
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
30-104 2.47e-04

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: 41.65  E-value: 2.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  30 AIQLISRMEYVHS---KNLIYRDVKPENFLIGRPGnktqQVIHIIDFGLAkeyidpeTKKHIPYREHKsltGTARYMS 104
Cdd:cd14058    95 ALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGG----TVLKICDFGTA-------CDISTHMTNNK---GSAAWMA 158
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1-77 2.60e-04

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: 41.95  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLEL--LGPSLEDLFDlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 77
Cdd:cd05060    72 LVMELapLGPLLKYLKK--RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL-----VNRHQAKISDFGMSR 143
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
32-141 2.76e-04

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: 41.99  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTKKHIPYREHKSLTGTARYMSINTHLGK 111
Cdd:cd06651   119 QILEGMSYLHSNMIVHRDIKGANILRDSAGN-----VKLGDFGASKRL----QTICMSGTGIRSVTGTPYWMSPEVISGE 189
                          90       100       110
                  ....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKA 141
Cdd:cd06651   190 GYGRKADVWSLGCTVVEMLTEKPPWAEYEA 219
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
1-104 2.78e-04

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: 41.65  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd06611    79 ILIEFCdGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD-----VKLADFGVSAKN 153
                          90       100
                  ....*....|....*....|....*
gi 1398130438  80 IDPETKKHipyrehkSLTGTARYMS 104
Cdd:cd06611   154 KSTLQKRD-------TFIGTPYWMA 171
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
27-78 2.93e-04

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: 41.59  E-value: 2.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  27 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKE 78
Cdd:cd05048   127 LHIAIQIAAGMEYLSSHHYVHRDLAARNCLVG-----DGLTVKISDFGLSRD 173
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
20-91 3.00e-04

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: 41.63  E-value: 3.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  20 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE--YID---PETKKHIPYR 91
Cdd:cd05053   129 QLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE-----DNVMKIADFGLARDihHIDyyrKTTNGRLPVK 200
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
1-213 3.11e-04

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: 41.53  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgpSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIHIIDFGLAke 78
Cdd:cd14195    85 LILELV--SGGELFDFLAEKESLteEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML-LDKNVPNPRIKLIDFGIA-- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 yidpetKKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWqglkadtlkeryqkIGDT 154
Cdd:cd14195   160 ------HKIEAGNEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPF--------------LGET 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 155 KRATPIEVLCENFPEMATYLRYVRRLdffekpDYDYLRKLFT-DLFDRKGYMFDYEYDWI 213
Cdd:cd14195   216 KQETLTNISAVNYDFDEEYFSNTSEL------AKDFIRRLLVkDPKKRMTIAQSLEHSWI 269
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-77 3.24e-04

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: 41.84  E-value: 3.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLCDRT----FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 77
Cdd:cd05574    87 ELFRLLQKQpgkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGH-----IMLTDFDLSK 151
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
18-144 3.51e-04

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: 41.54  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYidpetkKHIPYREhKSLT 97
Cdd:cd05098   129 EEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV-----TEDNVMKIADFGLARDI------HHIDYYK-KTTN 196
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1398130438  98 G--TARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05098   197 GrlPVKWMAPEALFDRIYTHQSDVWSFGvLLWEIFTLGGSPYPGVPVEEL 246
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
8-199 3.68e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 41.50  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   8 PSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPEtkk 86
Cdd:cd05102   156 QPRQEVDDLWQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPD--- 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  87 hipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADtlKERYQKIGDTKRATPievlce 165
Cdd:cd05102   228 ---YVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGvLLWEIFSLGASPYPGVQIN--EEFCQRLKDGTRMRA------ 296
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1398130438 166 nfPEMATYLRYVRRL-----DFFEKPDYDYLRKLFTDLF 199
Cdd:cd05102   297 --PEYATPEIYRIMLscwhgDPKERPTFSDLVEILGDLL 333
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
1-89 3.86e-04

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: 41.34  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEY 79
Cdd:cd14154    67 LITEYIpGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLV-----REDKTVVVADFGLARLI 141
                          90
                  ....*....|
gi 1398130438  80 IDPETKKHIP 89
Cdd:cd14154   142 VEERLPSGNM 151
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
7-76 4.02e-04

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: 41.16  E-value: 4.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLA 76
Cdd:cd14150    79 GSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFL-----HEGLTVKIGDFGLA 143
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
19-80 4.27e-04

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: 41.43  E-value: 4.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 80
Cdd:cd05590    91 RRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGH-----CKLADFGMCKEGI 147
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1-90 4.34e-04

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: 41.04  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPslEDLFDLCDRTFSLKT-VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTQQViHIIDFGLAKEy 79
Cdd:cd14108    75 IVTELCHE--ELLERITKRPTVCESeVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMA--DQKTDQV-RICDFGNAQE- 148
                          90
                  ....*....|.
gi 1398130438  80 IDPETKKHIPY 90
Cdd:cd14108   149 LTPNEPQYCKY 159
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
18-77 4.42e-04

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 41.56  E-value: 4.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTqqvIHIIDFGLAK 77
Cdd:PTZ00036  164 NHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI-DPNTHT---LKLCDFGSAK 219
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
15-77 4.62e-04

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 41.07  E-value: 4.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  15 DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTqqvIHIIDFGLAK 77
Cdd:cd05096   129 AHCLPAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLVG--ENLT---IKIADFGMSR 186
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-77 4.78e-04

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: 40.85  E-value: 4.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   9 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 77
Cdd:cd05068    89 SLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENN-----ICKVADFGLAR 152
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
22-77 4.78e-04

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: 41.07  E-value: 4.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 77
Cdd:cd05079   107 NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-----ESEHQVKIGDFGLTK 157
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
23-78 4.97e-04

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: 40.80  E-value: 4.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  23 LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 78
Cdd:cd05039   101 RKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDN-----VAKVSDFGLAKE 151
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
32-91 4.98e-04

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: 40.83  E-value: 4.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID---------------PETKKHIPYR 91
Cdd:cd14073   109 QIVSAVHYCHKNGVVHRDLKLENILLDQNGN-----AKIADFGLSNLYSKdkllqtfcgsplyasPEIVNGTPYQ 178
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
22-77 4.98e-04

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: 41.21  E-value: 4.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 77
Cdd:cd05038   107 DLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILV-----ESEDLVKISDFGLAK 157
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
32-104 5.30e-04

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: 40.85  E-value: 5.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEY--IDPETkkhipyrehKSLTGTARYMS 104
Cdd:cd06624   116 QILEGLKYLHDNKIVHRDIKGDNVLV----NTYSGVVKISDFGTSKRLagINPCT---------ETFTGTLQYMA 177
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
8-144 5.44e-04

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: 41.15  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   8 PSLEDLFDLC---DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-----EY 79
Cdd:cd05101   127 PGMEYSYDINrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV-----TENNVMKIADFGLARdinniDY 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  80 IDPETKKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05101   202 YKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLMWEIFTLGGSPYPGIPVEEL 257
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
14-82 5.54e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 41.22  E-value: 5.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  14 FDLCDRTFsLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDP 82
Cdd:PHA03210  258 FDWKDRPL-LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGK-----IVLGDFGTAMPFEKE 320
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
30-151 5.66e-04

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: 41.05  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHL 109
Cdd:cd05570   102 AAEICLALQFLHERGIIYRDLKLDNVLLDAEGH-----IKIADFGMCKEGIWGGNTTS-------TFCGTPDYIAPEILR 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 151
Cdd:cd05570   170 EQDYGFSVDWWALGVLLYEMLAGQSPFEG---DDEDELFEAI 208
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
32-85 6.00e-04

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: 41.14  E-value: 6.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAKeYIDPETK 85
Cdd:cd07849   114 QILRGLKYIHSANVLHRDLKPSNLLL----NTNCDL-KICDFGLAR-IADPEHD 161
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
19-77 6.70e-04

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 40.75  E-value: 6.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:cd05095   126 LTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK-----NYTIKIADFGMSR 179
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
18-104 6.97e-04

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: 40.79  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 97
Cdd:cd06644   104 DRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD-----IKLADFGVSAKNVKTLQRR-------DSFI 171

                  ....*..
gi 1398130438  98 GTARYMS 104
Cdd:cd06644   172 GTPYWMA 178
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
7-85 7.02e-04

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 39.56  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDlcdrTFSLKTVLMIAI-QLISRMeyvHSKNLIYRDVKPENFLIGRPGnktqqvIHIIDFGLAKEYIDPETK 85
Cdd:COG3642    40 GETLADLLE----EGELPPELLRELgRLLARL---HRAGIVHGDLTTSNILVDDGG------VYLIDFGLARYSDPLEDK 106
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
32-123 8.13e-04

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: 40.36  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKKHIPYrehkslTGTARYMSINTHLGK 111
Cdd:cd07848   108 QLIKAIHWCHKNDIVHRDIKPENLLI-----SHNDVLKLCDFGFARNLSEGSNANYTEY------VATRWYRSPELLLGA 176
                          90
                  ....*....|..
gi 1398130438 112 EQSRRDDLEALG 123
Cdd:cd07848   177 PYGKAVDMWSVG 188
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-90 8.40e-04

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: 40.40  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFD-LCDRTF-SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK------------ 77
Cdd:cd14167    87 ELFDrIVEKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSK--IMISDFGLSKiegsgsvmstac 164
                          90
                  ....*....|....*.
gi 1398130438  78 ---EYIDPETKKHIPY 90
Cdd:cd14167   165 gtpGYVAPEVLAQKPY 180
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
29-136 9.15e-04

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: 40.12  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpETKKHIPYRehKSLTGTARYMSINTH 108
Cdd:cd06648   108 VCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGR-----VKLSDFGFCA-----QVSKEVPRR--KSLVGTPYWMAPEVI 175
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 109 LGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06648   176 SRLPYGTEVDIWSLGIMVIEMVDGEPPY 203
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
22-84 9.17e-04

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: 40.10  E-value: 9.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnktqQVIHIIDFGLAKeYIDPET 84
Cdd:cd05056   105 DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSP-----DCVKLGDFGLSR-YMEDES 161
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
24-141 9.25e-04

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: 40.09  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  24 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeYIDPEtKKHIPYREHKSltgTARYM 103
Cdd:cd05057   109 QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV-----KTPNHVKITDFGLAK-LLDVD-EKEYHAEGGKV---PIKWM 178
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398130438 104 SINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKA 141
Cdd:cd05057   179 ALESIQYRIYTHKSDVWSYGvTVWELMTFGAKPYEGIPA 217
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
32-76 9.51e-04

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: 40.19  E-value: 9.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:cd14070   111 QLVSAVEHLHRAGVVHRDLKIENLLLDENDN-----IKLIDFGLS 150
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
1-102 9.61e-04

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: 40.20  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFS----LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLA 76
Cdd:cd07837    82 LVFEYLDTDLKKFIDSYGRGPHnplpAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLV----DKQKGLLKIADLGLG 157
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1398130438  77 KEYIDP-ETKKH----IPYREHKSLTGTARY 102
Cdd:cd07837   158 RAFTIPiKSYTHeivtLWYRAPEVLLGSTHY 188
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
32-169 9.62e-04

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: 40.37  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKKHIpyrehKSLTGTARYMSinTHLGK 111
Cdd:cd05621   159 EVVLALDAIHSMGLIHRDVKPDNMLLDKYGH-----LKLADFGTCMK-MDETGMVHC-----DTAVGTPDYIS--PEVLK 225
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438 112 EQ------SRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATpievlceNFPE 169
Cdd:cd05621   226 SQggdgyyGRECDWWSVGVFLFEMLVGDTPFY---ADSLVGTYSKIMDHKNSL-------NFPD 279
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
28-76 9.90e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 40.36  E-value: 9.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398130438  28 MIAIQ--LISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:PHA03212  184 ILAIErsVLRAIQYLHENRIIHRDIKAENIFINHPGD-----VCLGDFGAA 229
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
21-76 9.92e-04

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: 40.19  E-value: 9.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKN--LIYRDVKPENFLIGrpgnkTQQVIHIIDFGLA 76
Cdd:cd14036   105 FSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG-----NQGQIKLCDFGSA 157
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
1-123 1.01e-03

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: 40.41  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkEYI 80
Cdd:cd06633    98 LVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ-----VKLADFGSA-SIA 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  81 DPETkkhipyrehkSLTGTARYMSINTHLGKEQSRRD---DLEALG 123
Cdd:cd06633   172 SPAN----------SFVGTPYWMAPEVILAMDEGQYDgkvDIWSLG 207
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
16-123 1.02e-03

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: 40.00  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  16 LCD----RTFSLKTVLMIAIQLISRMEYVHS----------KNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYID 81
Cdd:cd14053    80 LCDylkgNVISWNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLL-----KSDLTACIADFGLALKFEP 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1398130438  82 petkkHIPYREHKSLTGTARYMSINTHLGKEQSRRD-----DLEALG 123
Cdd:cd14053   155 -----GKSCGDTHGQVGTRRYMAPEVLEGAINFTRDaflriDMYAMG 196
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
30-136 1.03e-03

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: 40.39  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  30 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHL 109
Cdd:cd05617   122 AAEICIALNFLHERGIIYRDLKLDNVLLDADGH-----IKLTDYGMCKEGLGPGDTT-------STFCGTPNYIAPEILR 189
                          90       100
                  ....*....|....*....|....*..
gi 1398130438 110 GKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd05617   190 GEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
27-83 1.05e-03

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: 40.37  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  27 LMIAIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFGLA-----------------KEYIDPE 83
Cdd:cd05601   111 LVLAIHSLHSMGYVH------RDIKPENILIDRTGH-----IKLADFGSAaklssdktvtskmpvgtPDYIAPE 173
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
19-151 1.08e-03

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: 39.73  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLA---KEYIDPETKKHIPYRehks 95
Cdd:cd05148    99 QVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGE-----DLVCKVADFGLArliKEDVYLSSDKKIPYK---- 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  96 ltGTARYMSINTHLgkeqSRRDDLEALGhMFMY--FLRGSLPWQGLkadTLKERYQKI 151
Cdd:cd05148   170 --WTAPEAASHGTF----STKSDVWSFG-ILLYemFTYGQVPYPGM---NNHEVYDQI 217
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-77 1.16e-03

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: 40.03  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  12 DLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktQQVIHIIDFGLAK 77
Cdd:cd14106    94 ELQTLLDEeeCLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFP--LGDIKLCDFGISR 159
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1-81 1.20e-03

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: 40.04  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLC----DRTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 75
Cdd:cd06616    82 ICMELMDISLDKFYKYVyevlDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGN-----IKLCDFGI 156

                  ....*.
gi 1398130438  76 AKEYID 81
Cdd:cd06616   157 SGQLVD 162
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
20-78 1.21e-03

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 40.01  E-value: 1.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  20 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKE 78
Cdd:cd05051   127 TLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVG-----PNYTIKIADFGMSRN 180
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-135 1.33e-03

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: 40.03  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSKN-LIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 107
Cdd:cd06649   108 VSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 173
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 108 HLGKEQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:cd06649   174 LQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
32-142 1.39e-03

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: 39.83  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYidPETKKHIPYRehkslTGTARYMSINTHLGK 111
Cdd:cd14094   117 QILEALRYCHDNNIIHRDVKPHCVLLASKENSAP--VKLGGFGVAIQL--GESGLVAGGR-----VGTPHFMAPEVVKRE 187
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKAD 142
Cdd:cd14094   188 PYGKPVDVWGCGVILFILLSGCLPFYGTKER 218
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
7-136 1.43e-03

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: 39.63  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKK 86
Cdd:cd14149    91 GSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLTVKIGDFGLATVKSRWSGSQ 165
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1398130438  87 HIpyrehKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd14149   166 QV-----EQPTGSILWMApevIRMQDNNPFSFQSDVYSYGIVLYELMTGELPY 213
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
23-76 1.43e-03

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: 39.73  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  23 LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLA 76
Cdd:cd14013   119 NVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIV----SEGDGQFKIIDLGAA 168
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
32-77 1.60e-03

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: 39.34  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 77
Cdd:cd06631   111 QILEGVAYLHNNNVIHRDIKGNNIMLMPNG-----VIKLIDFGCAK 151
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
22-77 1.73e-03

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 39.57  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 77
Cdd:cd05097   127 SIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGN-----HYTIKIADFGMSR 177
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
20-78 1.75e-03

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: 39.52  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  20 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 78
Cdd:cd05074   119 TLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT-----VCVADFGLSKK 172
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
32-213 1.80e-03

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: 39.63  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyIDPETKKHIPYrehkslTGTARYMSINTHLGK 111
Cdd:cd07876   131 QMLCGIKHLHSAGIIHRDLKPSNIVV-----KSDCTLKILDFGLAR--TACTNFMMTPY------VVTRYYRAPEVILGM 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLkERYQKIgdtkratpIEVLCENFPEMATYLRYVRRLDFFEKPDYDYL 191
Cdd:cd07876   198 GYKENVDIWSVGCIMGELVKGSVIFQG--TDHI-DQWNKV--------IEQLGTPSAEFMNRLQPTVRNYVENRPQYPGI 266
                         170       180
                  ....*....|....*....|..
gi 1398130438 192 RklFTDLFDRKGYMFDYEYDWI 213
Cdd:cd07876   267 S--FEELFPDWIFPSESERDKL 286
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
34-130 1.83e-03

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: 39.19  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  34 ISRMEYVhSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKKHIPYREHKSLT-GTARYMS---INTH 108
Cdd:cd14037   121 VAAMHYL-KPPLIHRDLKVENVLISDSGN-----YKLCDFGSATTKIlPPQTKQGVTYVEEDIKKyTTLQYRApemIDLY 194
                          90       100
                  ....*....|....*....|..
gi 1398130438 109 LGKEQSRRDDLEALGhMFMYFL 130
Cdd:cd14037   195 RGKPITEKSDIWALG-CLLYKL 215
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
31-150 1.83e-03

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: 39.62  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  31 IQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPEtkkhipyREHKSLTGTA--RYMSINTH 108
Cdd:cd05108   116 VQIAKGMNYLEDRRLVHRDLAARNVLV-----KTPQHVKITDFGLAKLLGAEE-------KEYHAEGGKVpiKWMALESI 183
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1398130438 109 LGKEQSRRDDLEALGHM---FMYFlrGSLPWQGLKADTLKERYQK 150
Cdd:cd05108   184 LHRIYTHQSDVWSYGVTvweLMTF--GSKPYDGIPASEISSILEK 226
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
23-81 1.98e-03

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: 39.14  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438  23 LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYID 81
Cdd:cd05084    94 VKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTE-----KNVLKISDFGMSREEED 147
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
32-80 2.07e-03

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: 38.93  E-value: 2.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYI 80
Cdd:cd14074   111 QIVSAISYCHKLHVVHRDLKPENVVF----FEKQGLVKLTDFGFSNKFQ 155
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
29-76 2.07e-03

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: 38.97  E-value: 2.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLA 76
Cdd:cd06607   106 ICHGALQGLAYLHSHNRIHRDVKAGNILLTEPG-----TVKLADFGSA 148
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1-97 2.12e-03

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 39.36  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 80
Cdd:PTZ00024   97 LVMDIMASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKG-----ICKIADFGLARRYG 170
                          90
                  ....*....|....*..
gi 1398130438  81 DPETKKHIPYREHKSLT 97
Cdd:PTZ00024  171 YPPYSDTLSKDETMQRR 187
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1-199 2.14e-03

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: 39.28  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGP-SLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE 78
Cdd:cd05069    83 IVTEFMGKgSLLDFLKEGDgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD-----NLVCKIADFGLARL 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  79 YIDPEtkkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLkadTLKERYQKIGDTKRA 157
Cdd:cd05069   158 IEDNE------YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGM---VNREVLEQVERGYRM 228
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1398130438 158 TPIEVLCENFPEMatyLRYVRRLDFFEKPDYDYLRKLFTDLF 199
Cdd:cd05069   229 PCPQGCPESLHEL---MKLCWKKDPDERPTFEYIQSFLEDYF 267
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
26-74 2.15e-03

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 39.26  E-value: 2.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  26 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRP-----------GNKTqQVIHIIDFG 74
Cdd:cd13981   108 AMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEicadwpgegenGWLS-KGLKLIDFG 166
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
7-75 2.22e-03

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: 38.87  E-value: 2.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKtqqvIHIIDFGL 75
Cdd:cd14063    80 GRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENGR----VVITDFGL 142
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
39-144 2.29e-03

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: 39.21  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  39 YVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIdpetkkhIPYREHKSLTGTARYMSINTHLGKEQSRRDD 118
Cdd:cd05615   126 FLHKKGIIYRDLKLDNVMLDSEGH-----IKIADFGMCKEHM-------VEGVTTRTFCGTPDYIAPEIIAYQPYGRSVD 193
                          90       100
                  ....*....|....*....|....*.
gi 1398130438 119 LEALGHMFMYFLRGSLPWQGLKADTL 144
Cdd:cd05615   194 WWAYGVLLYEMLAGQPPFDGEDEDEL 219
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
7-199 2.40e-03

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: 38.90  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPEtkk 86
Cdd:cd05070    88 GSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG-----NGLICKIADFGLARLIEDNE--- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  87 hipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLKADTLKERYQKigDTKRATPievlcE 165
Cdd:cd05070   160 ---YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMNNREVLEQVER--GYRMPCP-----Q 229
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1398130438 166 NFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLF 199
Cdd:cd05070   230 DCPiSLHELMIHCWKKDPEERPTFEYLQGFLEDYF 264
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
27-91 2.47e-03

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: 38.84  E-value: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  27 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-----YIDPETKKHIPYR 91
Cdd:cd05090   127 LHIAIQIAAGMEYLSSHFFVHKDLAARNILVGE-----QLHVKISDLGLSREiyssdYYRVQNKSLLPIR 191
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
9-163 2.53e-03

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: 38.88  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   9 SLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKEYIDPETKKHI 88
Cdd:cd14012    90 SLSELLDSVG-SVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTG--IVKLTDYSLGKTLLDMCSRGSL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  89 pyREHKSltgTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADT---------LKERYQ-------KIG 152
Cdd:cd14012   167 --DEFKQ---TYWLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLE--KYTSpnpvlvsldLSASLQdflskclSLD 239
                         170
                  ....*....|.
gi 1398130438 153 DTKRATPIEVL 163
Cdd:cd14012   240 PKKRPTALELL 250
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
1-77 2.55e-03

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: 39.20  E-value: 2.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   1 MVLELLGPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAK 77
Cdd:cd07851    97 LVTHLMGADLNNI--VKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV----NEDCEL-KILDFGLAR 166
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
1-123 2.59e-03

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: 38.88  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkEYI 80
Cdd:cd06635   102 LVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ-----VKLADFGSA-SIA 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  81 DPETkkhipyrehkSLTGTARYMSINTHLGKEQSRRD---DLEALG 123
Cdd:cd06635   176 SPAN----------SFVGTPYWMAPEVILAMDEGQYDgkvDVWSLG 211
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
32-77 2.63e-03

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: 38.93  E-value: 2.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 77
Cdd:cd07850   110 QMLCGIKHLHSAGIIHRDLKPSNIVV-----KSDCTLKILDFGLAR 150
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
32-139 2.64e-03

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: 38.88  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd06642   109 EILKGLDYLHSERKIHRDIKAANVLLSEQGD-----VKLADFGVAGQLTDTQIKRN-------TFVGTPFWMAPEVIKQS 176
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGL 139
Cdd:cd06642   177 AYDFKADIWSLGITAIELAKGEPPNSDL 204
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
1-92 2.65e-03

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: 38.84  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLgP--SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKe 78
Cdd:cd14205    84 LIMEYL-PygSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV-----ENENRVKIGDFGLTK- 156
                          90
                  ....*....|....
gi 1398130438  79 yIDPETKKHIPYRE 92
Cdd:cd14205   157 -VLPQDKEYYKVKE 169
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-74 2.73e-03

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: 38.68  E-value: 2.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  11 EDLFDLCDRTFSLKTVL--MIAIQLISRMEYVHSKNLIYRDVKPENFLIG-RPGNktqqvIHIIDFG 74
Cdd:cd14101    93 QDLFDYITERGALDESLarRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGD-----IKLIDFG 154
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-90 2.79e-03

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: 38.88  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKE---------------YIDPETKKHIPY 90
Cdd:cd14168   116 QVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESK--IMISDFGLSKMegkgdvmstacgtpgYVAPEVLAQKPY 187
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
24-140 2.83e-03

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl 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 its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 38.84  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  24 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIhIIDFGLAKEYIDPETkkhipYREHKSLTGTARYM 103
Cdd:cd05075   113 QMLVKFMTDIASGMEYLSSKNFIHRDLAARNCML----NENMNVC-VADFGLSKKIYNGDY-----YRQGRISKMPVKWI 182
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1398130438 104 SINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLK 140
Cdd:cd05075   183 AIESLADRVYTTKSDVWSFGvTMWEIATRGQTPYPGVE 220
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
21-135 2.85e-03

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: 38.88  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTA 100
Cdd:cd06640   101 FQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGD-----VKLADFGVAGQLTDTQIKR-------NTFVGTP 165
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1398130438 101 RYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:cd06640   166 FWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
38-102 2.87e-03

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: 38.75  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398130438  38 EYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidPETKKHIPYrehkSLTGTARY 102
Cdd:cd05599   115 ESIHKLGYIHRDIKPDNLLLDARGH-----IKLSDFGLCT----GLKKSHLAY----STVGTPDY 166
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
32-145 2.87e-03

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: 38.72  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHIIDFGLAKEyIDPEtkkhipyREHKSLTGTARYMSINTHLGK 111
Cdd:cd14114   108 QVCEGLCHMHENNIVHLDIKPENIMC---TTKRSNEVKLIDFGLATH-LDPK-------ESVKVTTGTAEFAAPEIVERE 176
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-TLK 145
Cdd:cd14114   177 PVGFYTDMWAVGVLSYVLLSGLSPFAGENDDeTLR 211
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
27-74 2.96e-03

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: 38.87  E-value: 2.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  27 LMIAIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFG 74
Cdd:cd05597   111 MVLAIDSIHQLGYVH------RDIKPDNVLLDRNGH-----IRLADFG 147
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
1-136 2.97e-03

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: 38.87  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELL-GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKey 79
Cdd:cd06658    96 VVMEFLeGGALTDI--VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR-----IKLSDFGFCA-- 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  80 idpETKKHIPYRehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06658   167 ---QVSKEVPKR--KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY 218
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
7-78 3.02e-03

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: 38.61  E-value: 3.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438   7 GPSLEDLFDlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHiiDFGLAKE 78
Cdd:cd14155    72 GGNLEQLLD-SNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVG--DFGLAEK 140
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-89 3.11e-03

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: 38.75  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  12 DLFDLC----DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL---IGRPGNktqqvIHIIDFGLAK------- 77
Cdd:cd14198    94 EIFNLCvpdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGD-----IKIVDFGMSRkighace 168
                          90       100
                  ....*....|....*....|
gi 1398130438  78 --------EYIDPETKKHIP 89
Cdd:cd14198   169 lreimgtpEYLAPEILNYDP 188
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
23-78 3.11e-03

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: 38.45  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  23 LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE 78
Cdd:cd05085    93 TKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGE-----NNALKISDFGMSRQ 143
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
37-136 3.14e-03

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: 38.86  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  37 MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGKEQSRR 116
Cdd:cd05618   134 LNYLHERGIIYRDLKLDNVLLDSEGH-----IKLTDYGMCKEGLRPGDTT-------STFCGTPNYIAPEILRGEDYGFS 201
                          90       100
                  ....*....|....*....|
gi 1398130438 117 DDLEALGHMFMYFLRGSLPW 136
Cdd:cd05618   202 VDWWALGVLMFEMMAGRSPF 221
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
16-77 3.14e-03

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: 38.69  E-value: 3.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438  16 LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQVIHIIDFGLAK 77
Cdd:cd13977   126 LLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISH--KRGEPILKVADFGLSK 185
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
23-59 3.16e-03

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: 38.54  E-value: 3.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1398130438  23 LKTVLMiaiQLISRMEYVHSKNLIYRDVKPENFLIGR 59
Cdd:cd14051   106 LKDLLL---QVAQGLKYIHSQNLVHMDIKPGNIFISR 139
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
7-83 3.18e-03

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: 38.36  E-value: 3.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPE 83
Cdd:cd14203    74 GSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVG-----DNLVCKIADFGLARLIEDNE 145
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
19-123 3.20e-03

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: 38.55  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  19 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYIDPETKKhipyreHKSLTG 98
Cdd:cd08529    96 RPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN-----VKIGDLGVAK-ILSDTTNF------AQTIVG 163
                          90       100
                  ....*....|....*....|....*
gi 1398130438  99 TARYMSINTHLGKEQSRRDDLEALG 123
Cdd:cd08529   164 TPYYLSPELCEDKPYNEKSDVWALG 188
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
29-123 3.50e-03

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: 38.57  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 107
Cdd:cd06615   104 ISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 169
                          90
                  ....*....|....*.
gi 1398130438 108 HLGKEQSRRDDLEALG 123
Cdd:cd06615   170 LQGTHYTVQSDIWSLG 185
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
7-126 3.63e-03

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: 38.40  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   7 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKK 86
Cdd:cd14221    74 GGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKS-----VVVADFGLARLMVDEKTQP 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1398130438  87 HIPYREHK-------SLTGTARYMSINTHLGKEQSRRDDLEALGHMF 126
Cdd:cd14221   149 EGLRSLKKpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1-77 3.66e-03

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: 38.37  E-value: 3.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130438   1 MVLELLGPSlEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAK 77
Cdd:cd14005    83 LIMERPEPC-QDLFDFITERGALseNLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI----NLRTGEVKLIDFGCGA 156
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
22-77 4.21e-03

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: 37.93  E-value: 4.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 77
Cdd:cd05083    98 PVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG-----VAKISDFGLAK 148
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-77 4.41e-03

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: 38.27  E-value: 4.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK 77
Cdd:cd14085   106 QILEAVAYLHENGIVHRDLKPENLLYATPAPDAP--LKIADFGLSK 149
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
32-135 4.52e-03

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: 38.13  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHLGK 111
Cdd:cd06641   109 EILKGLDYLHSEKKIHRDIKAANVLLSEHGE-----VKLADFGVAGQLTDTQIKRN-------*FVGTPFWMAPEVIKQS 176
                          90       100
                  ....*....|....*....|....
gi 1398130438 112 EQSRRDDLEALGHMFMYFLRGSLP 135
Cdd:cd06641   177 AYDSKADIWSLGITAIELARGEPP 200
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
21-136 4.60e-03

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: 38.18  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  21 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYidpETKKHIPYREHKSLTGTA 100
Cdd:cd06630   100 FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV----DSTGQRLRIADFGAAARL---ASKGTGAGEFQGQLLGTI 172
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1398130438 101 RYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 136
Cdd:cd06630   173 AFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
12-77 4.74e-03

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: 38.34  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438  12 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAK 77
Cdd:cd07879   105 DLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAV----NEDCE-LKILDFGLAR 165
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
18-77 4.81e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 38.32  E-value: 4.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  18 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIhIIDFGLAK 77
Cdd:PHA03209  151 SRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFI----NDVDQVC-IGDLGAAQ 205
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
29-92 5.08e-03

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 38.02  E-value: 5.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKE--------------YIDPETKKHIPYRE 92
Cdd:cd14067   119 IAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVQEHINIKLSDYGISRQsfhegalgvegtpgYQAPEIRPRIVYDE 196
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
1-95 6.10e-03

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: 38.01  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438   1 MVLELLGPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyI 80
Cdd:cd07880    97 LVMPFMGTDLGKLMKH--EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE-----LKILDFGLARQ-T 168
                          90
                  ....*....|....*
gi 1398130438  81 DPETKKHIPYREHKS 95
Cdd:cd07880   169 DSEMTGYVVTRWYRA 183
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
9-74 6.41e-03

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: 37.66  E-value: 6.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398130438   9 SLEDLFDLCDRT---FSLKTVLMIAIQLISRMEYVHSKNLI---YRDVKPENFLIGRPGnktqqVIHIIDFG 74
Cdd:cd13986    88 SLQDEIERRLVKgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDD-----EPILMDLG 154
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
1-76 6.44e-03

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: 37.69  E-value: 6.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130438   1 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLA 76
Cdd:cd06634    92 LVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPG-----LVKLGDFGSA 162
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
29-191 6.45e-03

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: 37.74  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  29 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPetkkhipyREHKSLTGTARYMS--- 104
Cdd:cd06618   119 MTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGN-----VKLCDFGISGRLVDS--------KAKTRSAGCAAYMAper 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438 105 INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTlkERYQKIGDTkrATPIEVLCENF-PEMATYLRYVRRLDFF 183
Cdd:cd06618   186 IDPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEF--EVLTKILNE--EPPSLPPNEGFsPDFCSFVDLCLTKDHR 261

                  ....*...
gi 1398130438 184 EKPDYDYL 191
Cdd:cd06618   262 YRPKYREL 269
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
29-74 6.47e-03

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: 36.27  E-value: 6.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFG 74
Cdd:cd13968    96 IMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN-----VKLIDFG 136
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
25-92 6.52e-03

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: 37.57  E-value: 6.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  25 TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyIDPETKKHIPYRE 92
Cdd:cd05081   109 RLLLYSSQICKGMEYLGSRRCVHRDLAARNILV-----ESEAHVKIADFGLAK--LLPLDKDYYVVRE 169
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
22-78 7.52e-03

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: 37.46  E-value: 7.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130438  22 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnkTQ-QVIHIIDFGLAKE 78
Cdd:cd05055   139 TLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL------THgKIVKICDFGLARD 190
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
32-75 7.53e-03

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: 37.72  E-value: 7.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 75
Cdd:cd05625   109 ELTCAVESVHKMGFIHRDIKPDNILIDRDGH-----IKLTDFGL 147
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
32-79 8.12e-03

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: 37.46  E-value: 8.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 79
Cdd:cd07836   108 QLLKGIAFCHENRVLHRDLKPQNLLINKRGE-----LKLADFGLARAF 150
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
32-138 8.29e-03

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: 37.15  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFL-IGRPGNktqqVIHIIDFGLAKEyIDPETKKHIPYRehksltgTARYMSINTHLG 110
Cdd:cd14104   105 QVCEALEFLHSKNIGHFDIRPENIIyCTRRGS----YIKIIEFGQSRQ-LKPGDKFRLQYT-------SAEFYAPEVHQH 172
                          90       100
                  ....*....|....*....|....*...
gi 1398130438 111 KEQSRRDDLEALGHMFMYFLRGSLPWQG 138
Cdd:cd14104   173 ESVSTATDMWSLGCLVYVLLSGINPFEA 200
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
29-76 8.73e-03

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: 37.09  E-value: 8.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1398130438  29 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:cd14027    95 IILEIIEGMAYLHGKGVIHKDLKPENILVDNDFH-----IKIADLGLA 137
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
32-77 9.55e-03

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: 37.38  E-value: 9.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398130438  32 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 77
Cdd:cd07874   127 QMLCGIKHLHSAGIIHRDLKPSNIVV-----KSDCTLKILDFGLAR 167
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
20-76 9.89e-03

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: 37.14  E-value: 9.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398130438  20 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 76
Cdd:cd05629    97 TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH-----IKLSDFGLS 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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