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Conserved domains on  [gi|919096895|ref|XP_013385115|]
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casein kinase I isoform X2 [Lingula anatina]

Protein Classification

casein kinase I( domain architecture ID 10197553)

casein kinase I (CKI) family protein is a serine/threonine-protein kinase which catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, similar to CKI-gamma isoforms

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0006468|GO:0004674|GO:0005524
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
46-333 0e+00

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: 663.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGP 125
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDFGLAKEYIDPETHKHI 205
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 206 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 285
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 286 EELATYLRYVRRLDFFETPDYDYLRKLFTDLMAKKGWECDWEFDWTGR 333
Cdd:cd14126  241 EEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
333-424 2.19e-32

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: 118.44  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  333 RQLSTPSGSIHTTEGATSPNRDgegrvRHnTQTNK------------QSNPRGTAWGEPQRP-NNYLGPNLTPADRHGGS 399
Cdd:pfam12605   1 KPMPTPVGSLQTSESAVSPSRE-----AH-IGVSRpplpqprrvsqqGSKGRKGAWPPPTPQtNAETLGSHLPADRHGGS 74
                          90       100
                  ....*....|....*....|....*
gi 919096895  400 VQVVSSTNGELAPDDPTAGHSNTPI 424
Cdd:pfam12605  75 VQVVSSTNGELNTDDPTAGHSNAPI 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 ...
46-333 0e+00

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: 663.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGP 125
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDFGLAKEYIDPETHKHI 205
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 206 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 285
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 286 EELATYLRYVRRLDFFETPDYDYLRKLFTDLMAKKGWECDWEFDWTGR 333
Cdd:cd14126  241 EEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
333-424 2.19e-32

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: 118.44  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  333 RQLSTPSGSIHTTEGATSPNRDgegrvRHnTQTNK------------QSNPRGTAWGEPQRP-NNYLGPNLTPADRHGGS 399
Cdd:pfam12605   1 KPMPTPVGSLQTSESAVSPSRE-----AH-IGVSRpplpqprrvsqqGSKGRKGAWPPPTPQtNAETLGSHLPADRHGGS 74
                          90       100
                  ....*....|....*....|....*
gi 919096895  400 VQVVSSTNGELAPDDPTAGHSNTPI 424
Cdd:pfam12605  75 VQVVSSTNGELNTDDPTAGHSNAPI 99
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
43-289 3.26e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.13  E-value: 3.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  43 VGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQ----LHLEYRFYKQLgQSEGVPQVYYFGPCGKYNA 117
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKvLRPELAADPEarerFRREARALARL-NHPNIVRVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEy 196
Cdd:COG0515   84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR-----VKLIDFGIARA- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 IDPETHKHipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGdTKRATP 276
Cdd:COG0515  157 LGGATLTQ-----TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG---DSPAELLRAHL-REPPPP 227
                        250
                 ....*....|...
gi 919096895 277 IEVLCENFPEELA 289
Cdd:COG0515  228 PSELRPDLPPALD 240
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
47-288 7.73e-31

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.17  E-value: 7.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895    47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL 123
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   124 gpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEYIDPET 201
Cdd:smart00220  80 --EGGDLFDLLKKRgrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-----DEDGHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   202 hkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRATPIEVlc 281
Cdd:smart00220 153 --------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPE-- 220

                   ....*..
gi 919096895   282 ENFPEEL 288
Cdd:smart00220 221 WDISPEA 227
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
42-313 3.71e-26

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 107.34  E-value: 3.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  42 MVGPNFRVGKKIGCGNFG---ELRLGKNLYNNEHVAIKLEPMKSRApqLHLEYRFYKQLGQSE--------------GVP 104
Cdd:PHA02882   9 ITGKEWKIDKLIGCGGFGcvyETQCASDHCINNQAVAKIENLENET--IVMETLVYNNIYDIDkialwknihnidhlGIP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 105 QVY---YFGPCGKY-NALVLELLGPSLEDLFD--LCDRKFSLKTvlmIAIQLVTRMEYVHSKHLIYRDVKPENFLI-GRQ 177
Cdd:PHA02882  87 KYYgcgSFKRCRMYyRFILLEKLVENTKEIFKriKCKNKKLIKN---IMKDMLTTLEYIHEHGISHGDIKPENIMVdGNN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 178 SAkkqhiiYIIDFGLAKEYIdpeTH-KHIPY-REHKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:PHA02882 164 RG------YIIDYGIASHFI---IHgKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWK 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 255 GLKADTLKERYQKIGDTKRATPIEVLCENFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:PHA02882 235 GFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIF 293
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
50-204 2.86e-12

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: 66.37  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   50 GKKIGCGNFGELRLGK----NLYNNEHVAIKLepMKSRAPQLHL-----EYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKT--LKEGADEEERedfleEASIMKKL-DHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  121 ELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDFGLAKE-YID 198
Cdd:pfam07714  81 EYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE-----NLVVKISDFGLSRDiYDD 155

                  ....*.
gi 919096895  199 PETHKH 204
Cdd:pfam07714 156 DYYRKR 161
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
48-255 2.33e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.42  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  48 RVGKKIGCGNFGELRLGKNLYNNEHVAIKLepmksrapqLHLEY--------RFYKQlGQS------EGVPQVYYFGPCG 113
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKV---------LRPDLardpefvaRFRRE-AQSaaslshPNIVSVYDVGEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 KYNALVLELL-GPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGL 192
Cdd:NF033483  80 GIPYIVMEYVdGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK-----VTDFGI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 193 AKEYidPEThkhipyrehkSLT------GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 255
Cdd:NF033483 154 ARAL--SST----------TMTqtnsvlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
 
Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
46-333 0e+00

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: 663.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGP 125
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDFGLAKEYIDPETHKHI 205
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 206 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 285
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 286 EELATYLRYVRRLDFFETPDYDYLRKLFTDLMAKKGWECDWEFDWTGR 333
Cdd:cd14126  241 EEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
46-313 7.50e-171

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: 480.03  E-value: 7.50e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGP 125
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQsaKKQHIIYIIDFGLAKEYIDPETHKHI 205
Cdd:cd14016   81 SLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLG--KNSNKVYLIDFGLAKKYRDPRTGKHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 206 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 285
Cdd:cd14016  159 PYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSPEELCKGLP 238
                        250       260
                 ....*....|....*....|....*...
gi 919096895 286 EELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14016  239 KEFAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
47-322 2.79e-159

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: 451.05  E-value: 2.79e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPS 126
Cdd:cd14125    2 YRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsAKKQHIIYIIDFGLAKEYIDPETHKHIP 206
Cdd:cd14125   82 LEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGL--GKKGNLVYIIDFGLAKKYRDPRTHQHIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 207 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE 286
Cdd:cd14125  160 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPS 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 919096895 287 ELATYLRYVRRLDFFETPDYDYLRKLFTDLMAKKGW 322
Cdd:cd14125  240 EFATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
47-321 8.86e-149

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: 424.60  E-value: 8.86e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPS 126
Cdd:cd14127    2 YKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDFGLAKEYIDPETHKHIP 206
Cdd:cd14127   82 LEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTKNANVIHVVDFGMAKQYRDPKTKQHIP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 207 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE 286
Cdd:cd14127  162 YREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPIRDLCEGFPE 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 919096895 287 ELATYLRYVRRLDFFETPDYDYLRKLFTDLMAKKG 321
Cdd:cd14127  242 EFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
47-313 8.11e-122

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: 355.66  E-value: 8.11e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPS 126
Cdd:cd14128    2 YRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFL--IGRQSAKkqhiIYIIDFGLAKEYIDPETHKH 204
Cdd:cd14128   82 LEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLmgIGRHCNK----LFLIDFGLAKKYRDSRTRQH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 205 IPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENF 284
Cdd:cd14128  158 IPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGF 237
                        250       260
                 ....*....|....*....|....*....
gi 919096895 285 PEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14128  238 PAEFAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
46-314 2.53e-73

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: 231.38  E-value: 2.53e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGP 125
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLF-DLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkQHIIYIIDFGLAKEYIDPETHKH 204
Cdd:cd14017   81 NLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSD-ERTVYILDFGLARQYTNKDGEVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 205 IPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKadtlkeRYQKIGDTKRATPIEVLCENF 284
Cdd:cd14017  160 RPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKIDHEELLKGL 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 919096895 285 PEELATYLRYVRRLDFFETPDYDYLRKLFT 314
Cdd:cd14017  234 PKEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
42-313 2.39e-49

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: 170.15  E-value: 2.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  42 MVGPNFRVGKKIGCGNFGELRL------GKNLYNNEHVaIKLEPmKSRAPqLHLEYRFYKQLGQSE-------------- 101
Cdd:cd14015    7 VTKRQWKLGKSIGQGGFGEIYLasddstLSVGKDAKYV-VKIEP-HSNGP-LFVEMNFYQRVAKPEmikkwmkakklkhl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 102 GVPQVYYFG----PCGKYNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQ 177
Cdd:cd14015   84 GIPRYIGSGsheyKGEKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 178 SAKKQhiIYIIDFGLAKEYIDpeTHKHIPYRE--HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14015  164 KNKDQ--VYLVDYGLASRYCP--NGKHKEYKEdpRKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWED 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 256 LKADTLKERYQKIgdtKRATPIEVL---C---ENFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14015  240 NLKNPEYVQKQKE---KYMDDIPLLlkkCfpgKDVPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
47-313 6.94e-39

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: 141.34  E-value: 6.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLgqsEGVPQVYYFGPCGK---YNALVLELL 123
Cdd:cd14129    2 WKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKL---QGKDHVCRFIGCGRndrFNYVVMQLQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIiYIIDFGLAKEYIDPETH 202
Cdd:cd14129   79 GRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKC-YMLDFGLARQFTNSCGD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KHIPyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATPIEVLCE 282
Cdd:cd14129  158 VRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYEHRLMLK 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 919096895 283 NFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14129  231 HLPPEFSVFLDHISGLDYFTKPDYQLLVSVF 261
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
47-313 8.09e-39

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: 141.32  E-value: 8.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLgqsEGVPQVYYFGPCG---KYNALVLELL 123
Cdd:cd14130    2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKL---QGKDHVCRFIGCGrneKFNYVVMQLQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIiYIIDFGLAKEYIDpETH 202
Cdd:cd14130   79 GRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKC-YMLDFGLARQYTN-TTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATPIEVLCE 282
Cdd:cd14130  157 EVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK------EQVGMIKEKYEHRMLLK 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 919096895 283 NFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14130  231 HMPSEFHLFLDHIASLDYFTKPDYQLIMSVF 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
53-246 7.86e-35

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: 128.93  E-value: 7.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL-GPSLE 128
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKvipKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCeGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEYIDPETHKHIPYR 208
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL-----DSDGTVKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 919096895 209 ehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYF 246
Cdd:cd00180  155 -----TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
333-424 2.19e-32

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: 118.44  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  333 RQLSTPSGSIHTTEGATSPNRDgegrvRHnTQTNK------------QSNPRGTAWGEPQRP-NNYLGPNLTPADRHGGS 399
Cdd:pfam12605   1 KPMPTPVGSLQTSESAVSPSRE-----AH-IGVSRpplpqprrvsqqGSKGRKGAWPPPTPQtNAETLGSHLPADRHGGS 74
                          90       100
                  ....*....|....*....|....*
gi 919096895  400 VQVVSSTNGELAPDDPTAGHSNTPI 424
Cdd:pfam12605  75 VQVVSSTNGELNTDDPTAGHSNAPI 99
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
47-313 5.43e-32

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: 123.84  E-value: 5.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLG-----KNLYNNEHVAIKLEPmkSRAPQLHLEYRFYKQLGQSE--------------GVPQVY 107
Cdd:cd14122   12 WKLGLPIGQGGFGRLYLAdenssESVGSDAPYVVKVEP--SDNGPLFTELKFYMRAAKPDqiqkwikshklkylGVPKYW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 108 YFGPCGK----YNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQH 183
Cdd:cd14122   90 GSGLHEKngksYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLL---SYKNPD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 184 IIYIIDFGLAKEYIDPETHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 263
Cdd:cd14122  167 QVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWEDNLKDPNYV 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 919096895 264 RYQKIGDTKRATPIEVLC---ENFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:cd14122  247 RDSKIRYRDNISELMEKCfpgKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
43-289 3.26e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 125.13  E-value: 3.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  43 VGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQ----LHLEYRFYKQLgQSEGVPQVYYFGPCGKYNA 117
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKvLRPELAADPEarerFRREARALARL-NHPNIVRVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEy 196
Cdd:COG0515   84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR-----VKLIDFGIARA- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 IDPETHKHipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGdTKRATP 276
Cdd:COG0515  157 LGGATLTQ-----TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG---DSPAELLRAHL-REPPPP 227
                        250
                 ....*....|...
gi 919096895 277 IEVLCENFPEELA 289
Cdd:COG0515  228 PSELRPDLPPALD 240
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
47-288 7.73e-31

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.17  E-value: 7.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895    47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL 123
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   124 gpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEYIDPET 201
Cdd:smart00220  80 --EGGDLFDLLKKRgrLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-----DEDGHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   202 hkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRATPIEVlc 281
Cdd:smart00220 153 --------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPE-- 220

                   ....*..
gi 919096895   282 ENFPEEL 288
Cdd:smart00220 221 WDISPEA 227
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
46-293 3.78e-30

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: 117.69  E-value: 3.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHL----EYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKvLRPELAEDEEFRErflrEARALARL-SHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL-GPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEyIDP 199
Cdd:cd14014   80 EYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG-----RVKLTDFGIARA-LGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 200 ETHKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIgdTKRATPIEV 279
Cdd:cd14014  153 SGLTQT-----GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDG--DSPAAVLAKHL--QEAPPPPSP 223
                        250
                 ....*....|....
gi 919096895 280 LCENFPEELATYLR 293
Cdd:cd14014  224 LNPDVPPALDAIIL 237
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
42-314 5.16e-28

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: 113.02  E-value: 5.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  42 MVGPNFRVGKKIGCGNFGELRLGKNLYNN------EHVaIKLEPMKSrAPqLHLEYRFYKQLGQSE-------------- 101
Cdd:cd14123    9 TEKKNWRLGKMIGKGGFGLIYLASPQVNVpveddaVHV-IKVEYHEN-GP-LFSELKFYQRAAKPDtiskwmkskqldyl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 102 GVPQVYYFGPC----GKYNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRq 177
Cdd:cd14123   86 GIPTYWGSGLTefngTSYRFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 178 saKKQHIIYIIDFGLAKEYIDPETHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW---- 253
Cdd:cd14123  165 --RNPNEVYLADYGLSYRYCPNGNHKEYKENPRKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeqnl 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 254 ------QGLKADTLKERYQKIgdTKRATPIEVLCenfpeELATYLRYVRRLDFFETPDYDYLRKLFT 314
Cdd:cd14123  243 knpvavQEAKAKLLSNLPDSV--LKWSTGGSSSM-----EIAQFLSRVKDLAYDEKPDYQALKKILS 302
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
102-311 4.84e-27

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: 109.93  E-value: 4.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 102 GVPQVYYFGPCGKYNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKK 181
Cdd:cd14124   83 GIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFV---DPED 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 182 QHIIYIIDFGLAKEYIdpETHKHIPYRE-HKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKAD 259
Cdd:cd14124  160 QSEVYLAGYGFAFRYC--PGGKHVEYREgSRSPhEGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHN 237
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 260 T-----LKERYqkigdtkRATPIEVLCENF-----PEELATYLRYVRRLDFFETPDYDYLRK 311
Cdd:cd14124  238 TedimkQKERF-------MDDVPGFLGPCFhqkkvSEALQKYLKVVMALQYEEKPDYAMLRN 292
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
42-313 3.71e-26

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 107.34  E-value: 3.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  42 MVGPNFRVGKKIGCGNFG---ELRLGKNLYNNEHVAIKLEPMKSRApqLHLEYRFYKQLGQSE--------------GVP 104
Cdd:PHA02882   9 ITGKEWKIDKLIGCGGFGcvyETQCASDHCINNQAVAKIENLENET--IVMETLVYNNIYDIDkialwknihnidhlGIP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 105 QVY---YFGPCGKY-NALVLELLGPSLEDLFD--LCDRKFSLKTvlmIAIQLVTRMEYVHSKHLIYRDVKPENFLI-GRQ 177
Cdd:PHA02882  87 KYYgcgSFKRCRMYyRFILLEKLVENTKEIFKriKCKNKKLIKN---IMKDMLTTLEYIHEHGISHGDIKPENIMVdGNN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 178 SAkkqhiiYIIDFGLAKEYIdpeTH-KHIPY-REHKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:PHA02882 164 RG------YIIDYGIASHFI---IHgKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWK 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 255 GLKADTLKERYQKIGDTKRATPIEVLCENFPEELATYLRYVRRLDFFETPDYDYLRKLF 313
Cdd:PHA02882 235 GFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIF 293
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
46-268 1.92e-21

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: 93.31  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRA-PQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidKKKLKSEDeEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LL--GpsleDLFD-LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKEYI 197
Cdd:cd05117   80 LCtgG----ELFDrIVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILL--ASKDPDSPIKIIDFGLAKIFE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 198 DPEthkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMYF-LRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd05117  154 EGE--------KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLG-VILYIlLCGYPPFYG---ETEQELFEKI 213
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
47-200 2.90e-20

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: 89.60  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKlepmKSRAPQLHL-----EYRFYKQLGQSEGVPQV-----YYFGPCGKYN 116
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIK----KIKNDFRHPkaalrEIKLLKHLNDVEGHPNIvklldVFEHRGGNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiIYIIDFGLAKEY 196
Cdd:cd05118   77 CLVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ----LKLADFGLARSF 152

                 ....
gi 919096895 197 IDPE 200
Cdd:cd05118  153 TSPP 156
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
46-286 1.82e-18

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: 84.96  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEpmKSR------APQLHLEYRFYKQLGqSEGVPQVY---------YF 109
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKvLD--KRHiikekkVKYVTIEKEVLSRLA-HPGIVKLYytfqdesklYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 110 gpcgkynalVLELL--GPSLEDLfdlcdRK---FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHI 184
Cdd:cd05581   79 ---------VLEYApnGDLLEYI-----RKygsLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD----EDMHI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 185 IyIIDFGLAK----------EYIDPETHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd05581  141 K-ITDFGTAKvlgpdsspesTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR 219
                        250       260       270
                 ....*....|....*....|....*....|..
gi 919096895 255 GlkaDTLKERYQKIgdTKRATPIevlCENFPE 286
Cdd:cd05581  220 G---SNEYLTFQKI--VKLEYEF---PENFPP 243
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
46-268 3.06e-18

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: 84.11  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIidksKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENKIYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLgpSLEDLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEYidp 199
Cdd:cd14003   80 YA--SGGELFDYIvnNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD-----KNGNLKIIDFGLSNEF--- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 200 ethkhIPYREHKSLTGTARYMS---INTH--LGKEQsrrdDLEALGHMfMYF-LRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd14003  150 -----RGGSLLKTFCGTPAYAApevLLGRkyDGPKA----DVWSLGVI-LYAmLTGYLPFDD---DNDSKLFRKI 211
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
118-268 4.21e-16

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: 77.56  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL--GpsleDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLA 193
Cdd:cd05123   70 LVLDYVpgG----ELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDG----HIK-LTDFGLA 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 194 KEYIDPETHKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 268
Cdd:cd05123  141 KELSSDGDRTY-------TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVL-LYeMLTGKPPFY---AENRKEIYEKI 205
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
46-253 7.81e-16

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: 77.18  E-value: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK----LEPMKSRAPQLHLEYRFYKQLgQSEGVpqVYYFGPC---GKYNaL 118
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKevelSGDSEEELEALEREIRILSSL-KHPNI--VRYLGTErteNTLN-I 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELL-GPSLEDLfdLCD-RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEY 196
Cdd:cd06606   77 FLEYVpGGSLASL--LKKfGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG-----VVKLADFGCAKRL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 197 IDPETHKhipyrEHKSLTGTARYMS---INthlGKEQSRRDDLEALG----HMFMyflrGSLPW 253
Cdd:cd06606  150 AEIATGE-----GTKSLRGTPYWMApevIR---GEGYGRAADIWSLGctviEMAT----GKPPW 201
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
53-221 2.71e-15

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: 75.27  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKnlYNNEHVAIKLepMKSRapqlHLEYRFYKQLgQSEgVPQ---------VYYFGPC--GKYNALVLE 121
Cdd:cd13999    1 IGSGSFGEVYKGK--WRGTDVAIKK--LKVE----DDNDELLKEF-RRE-VSIlsklrhpniVQFIGAClsPPPLCIVTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQ-SAKkqhiiyIIDFGLAKEyidp 199
Cdd:cd13999   71 YMpGGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENfTVK------IADFGLSRI---- 140
                        170       180
                 ....*....|....*....|..
gi 919096895 200 ethKHIPYREHKSLTGTARYMS 221
Cdd:cd13999  141 ---KNSTTEKMTGVVGTPRWMA 159
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
46-268 1.92e-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: 73.38  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKlepMKSRAPQLHL--------EYRFYKQLGQSEGVPQVYYFGPCgKYNA 117
Cdd:cd05580    2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALK---ILKKAKIIKLkqvehvlnEKRILSEVRHPFIVNLLGSFQDD-RNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL--GpsleDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLA 193
Cdd:cd05580   78 MVMEYVpgG----ELFSLLRRsgRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDG----H-IKITDFGFA 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 194 KeYIDPETHkhipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKI 268
Cdd:cd05580  149 K-RVKDRTY---------TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF---FDENPMKIYEKI 210
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
46-268 3.01e-14

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: 73.86  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKIlrksDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLGPSleDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYID- 198
Cdd:cd05573   82 YMPGG--DLMNLLIKYdvFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADG----H-IKLADFGLCTKMNKs 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 199 --------------------PETHKHIPYREH-KSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPwqgL 256
Cdd:cd05573  155 gdresylndsvntlfqdnvlARRRPHKQRRVRaYSAVGTPDYIAPEVLRGTGYGPECDWWSLG-VILYeMLYGFPP---F 230
                        250
                 ....*....|..
gi 919096895 257 KADTLKERYQKI 268
Cdd:cd05573  231 YSDSLVETYSKI 242
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
149-287 6.41e-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: 71.49  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKeyidpethKHIPYREHKSLTGTARYMSINTHLGK 228
Cdd:cd05572  101 CVVLAFEYLHSRGIIYRDLKPENLLLD-----SNGYVKLVDFGFAK--------KLGSGRKTWTFCGTPEYVAPEIILNK 167
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 229 EQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKeRYQKIGD-----------TKRATP-IEVLCENFPEE 287
Cdd:cd05572  168 GYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMK-IYNIILKgidkiefpkyiDKNAKNlIKQLLRRNPEE 237
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
46-268 9.06e-14

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: 70.97  E-value: 9.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKsrapQLhLEYRFYKQLgQSE----------GVPQVY-YFgpcgk 114
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKS----QL-QKSGLEHQL-RREieiqshlrhpNILRLYgYF----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNA----LVLELLgpSLEDLFDL--CDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYII 188
Cdd:cd14007   70 EDKkriyLILEYA--PNGELYKElkKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG-----SNGELKLA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 189 DFGLAkeyidpethKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQK 267
Cdd:cd14007  143 DFGWS---------VHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLG-VLCYeLLVGKPPF---ESKSHQETYKR 209

                 .
gi 919096895 268 I 268
Cdd:cd14007  210 I 210
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
50-253 1.82e-13

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: 70.41  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRA-PQLHLEY------------RFYkqlgqseGVP----QVYYF 109
Cdd:cd06626    5 GNKIGEGTFGKVYTAVNLDTGELMAmkeIRFQDNDPKTiKEIADEMkvlegldhpnlvRYY-------GVEvhreEVYIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 110 gpcgkynalvLELL-GPSLEDLFD-------LCDRKFslktvlmiAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakk 181
Cdd:cd06626   78 ----------MEYCqEGTLEELLRhgrildeAVIRVY--------TLQLLEGLAYLHENGIVHRDIKPANIFLDSNG--- 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 182 qhIIYIIDFGLAKEYIDPEThkHIPYREHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06626  137 --LIKLGDFGSAVKLKNNTT--TMAPGEVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
46-279 2.50e-13

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: 69.60  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEpMKSRAPQLHLEYRFYKQLGQSEGV--PQV-----YYFGPCGKYnaL 118
Cdd:cd14116    6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVL-FKAQLEKAGVEHQLRREVEIQSHLrhPNIlrlygYFHDATRVY--L 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELlGPSLEDLFDL--CDRKFSLKTVLMIaIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAkey 196
Cdd:cd14116   83 ILEY-APLGTVYRELqkLSKFDEQRTATYI-TELANALSYCHSKRVIHRDIKPENLLLGSAGELK-----IADFGWS--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 idpethKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATP 276
Cdd:cd14116  153 ------VHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFE---ANTYQETYKRISRVEFTFP 223

                 ...
gi 919096895 277 IEV 279
Cdd:cd14116  224 DFV 226
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
51-268 7.35e-13

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: 68.28  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEP-----MKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELL-G 124
Cdd:cd05611    2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKksdmiAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLnG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSLEDLFDLCDrKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPethkh 204
Cdd:cd05611   82 GDCASLIKTLG-GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLK-----LTDFGLSRNGLEK----- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 205 ipyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 268
Cdd:cd05611  151 ---RHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH---AETPDAVFDNI 208
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
46-264 8.48e-13

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: 67.93  E-value: 8.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAP----QLHLEYRFYKQLGQSEGVpQVYYFGPCGKYNALVLE 121
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPsslqKLFREVRIMKILNHPNIV-KLFEVIETEKTLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LlgPSLEDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYidp 199
Cdd:cd14072   80 Y--ASGGEVFDylVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN-----IKIADFGFSNEF--- 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 200 ethkhIPYREHKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 264
Cdd:cd14072  150 -----TPGNKLDTFCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRER 210
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
47-221 8.72e-13

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: 68.06  E-value: 8.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLgQSEGVpqVYYFGPCGKYNAL--VLELLG 124
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQC-DSPYI--VKYYGSYFKNTDLwiVMEYCG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 P-SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDpethk 203
Cdd:cd06612   82 AgSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAK-----LADFGVSGQLTD----- 151
                        170
                 ....*....|....*...
gi 919096895 204 hiPYREHKSLTGTARYMS 221
Cdd:cd06612  152 --TMAKRNTVIGTPFWMA 167
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
46-221 1.27e-12

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: 67.76  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK----------LEPMKSRAPQLHlEYRFYKQLGQSEGVPQVYYFGPCGKY 115
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKclyksgpnskDGNDFQKLPQLR-EIDLHRRVSRHPNIITLHDVFETEVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 116 NALVLELLgpSLEDLFDLC--DRKFSLKTVLM--IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiIYIIDFG 191
Cdd:cd13993   80 IYIVLEYC--PNGDLFEAIteNRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT----VKLCDFG 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 919096895 192 LAkeyidpeTHKHIPYrehKSLTGTARYMS 221
Cdd:cd13993  154 LA-------TTEKISM---DFGVGSEFYMA 173
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
50-208 1.38e-12

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 67.56  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895    50 GKKIGCGNFGELRLGKNLYNNEH----VAIKLepMKSRAPQLHL-----EYRFYKQLgQSEGVpqVYYFGPCGKYNAL-- 118
Cdd:smart00219   4 GKKLGEGAFGEVYKGKLKGKGGKkkveVAVKT--LKEDASEQQIeeflrEARIMRKL-DHPNV--VKLLGVCTEEEPLyi 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   119 VLELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAK--- 194
Cdd:smart00219  79 VMEYMeGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG-----ENLVVKISDFGLSRdly 153
                          170
                   ....*....|....*.
gi 919096895   195 --EYIDpETHKHIPYR 208
Cdd:smart00219 154 ddDYYR-KRGGKLPIR 168
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
52-250 1.60e-12

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: 67.74  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIKLEPMKSR----APQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPSL 127
Cdd:cd07832    7 RIGEGAHGIVFKAKDRETGETVALKKVALRKLeggiPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLSSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPethkhiPY 207
Cdd:cd07832   87 SEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLK-----IADFGLARLFSEE------DP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 919096895 208 REHKSLTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGS 250
Cdd:cd07832  156 RLYSHQVATRWYRAPELLYGSRKyDEGVDLWAVGCIFAELLNGS 199
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
53-295 1.78e-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: 67.34  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLY-NNEHVAIKLEPMKSRAPQLHL---EYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL-GPSL 127
Cdd:cd14202   10 IGHGAFAVVFKGRHKEkHDLEVAVKCINKKNLAKSQTLlgkEIKILKEL-KHENIVALYDFQEIANSVYLVMEYCnGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI----GRQSAKKQHIIYIIDFGLAKeYIDPETHK 203
Cdd:cd14202   89 ADYLH-TMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIADFGFAR-YLQNNMMA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 204 hipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKigdTKRATPievlceN 283
Cdd:cd14202  167 -------ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEK---NKSLSP------N 230
                        250
                 ....*....|..
gi 919096895 284 FPEELATYLRYV 295
Cdd:cd14202  231 IPRETSSHLRQL 242
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
136-312 2.01e-12

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: 67.46  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYIDpethkhipyrEHKSLTG 215
Cdd:cd05612   96 GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEG----H-IKLTDFGFAKKLRD----------RTWTLCG 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 216 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIgdtkratpievlcenfpeeLATYLRYV 295
Cdd:cd05612  161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD---DNPFGIYEKI-------------------LAGKLEFP 218
                        170
                 ....*....|....*..
gi 919096895 296 RRLDFFETpdyDYLRKL 312
Cdd:cd05612  219 RHLDLYAK---DLIKKL 232
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
129-210 2.40e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 66.80  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsAKKQhiIYIIDFGLAK------------ 194
Cdd:PHA03390  95 DLFDLLkkEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR--AKDR--IYLCDYGLCKiigtpscydgtl 170
                         90
                 ....*....|....*.
gi 919096895 195 EYIDPETHKHIPYREH 210
Cdd:PHA03390 171 DYFSPEKIKGHNYDVS 186
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
47-191 2.70e-12

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: 66.52  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQ-----SEGVPQVY---YFgpcgkYNA 117
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKiIKNNKDYLDQSLDEIRLLELLNKkdkadKYHIVRLKdvfYF-----KNH 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 118 L--VLELLGPSLEDLFDLcDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYIIDFG 191
Cdd:cd14133   76 LciVFELLSQNLYEFLKQ-NKFqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ---IKIIDFG 149
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
50-204 2.86e-12

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: 66.37  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   50 GKKIGCGNFGELRLGK----NLYNNEHVAIKLepMKSRAPQLHL-----EYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKT--LKEGADEEERedfleEASIMKKL-DHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  121 ELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDFGLAKE-YID 198
Cdd:pfam07714  81 EYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE-----NLVVKISDFGLSRDiYDD 155

                  ....*.
gi 919096895  199 PETHKH 204
Cdd:pfam07714 156 DYYRKR 161
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
46-257 3.02e-12

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: 66.46  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQL--GQSEGVPQVY--YFGPCgkYNALVLE 121
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLrsCESPYVVKCYgaFYKEG--EISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LL-GPSLEDLFDLCdRKFSLKTVLMIAIQLVTRMEYVHSK-HLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAkeyidp 199
Cdd:cd06623   80 YMdGGSLADLLKKV-GKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVK-----IADFGIS------ 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 200 ethKHIPYR--EHKSLTGTARYMS---INthlGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 257
Cdd:cd06623  148 ---KVLENTldQCNTFVGTVTYMSperIQ---GESYSYAADIWSLGLTLLECALGKFPFLPPG 204
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
47-193 3.07e-12

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: 67.59  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLhlEYRFYKQLGQS--EGVPQV--------YYFGPCg 113
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIirnVEKYREAAKI--EIDVLETLAEKdpNGKSHCvqlrdwfdYRGHMC- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 kynaLVLELLGPSLED-LFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI------------GRQSAK 180
Cdd:cd14134   91 ----IVFELLGPSLYDfLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynpkKKRQIR 166
                        170
                 ....*....|....*
gi 919096895 181 --KQHIIYIIDFGLA 193
Cdd:cd14134  167 vpKSTDIKLIDFGSA 181
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
47-195 4.24e-12

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: 66.40  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKlePMKSRAPQLH----L-EYRFYKQLGQSEGVPQVY---------YFgpc 112
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIK--KMKKKFYSWEecmnLrEVKSLRKLNEHPNIVKLKevfrendelYF--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 gkynalVLELLGPSLEDLF-DLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFG 191
Cdd:cd07830   76 ------VFEYMEGNLYQLMkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV-----SGPEVVKIADFG 144

                 ....
gi 919096895 192 LAKE 195
Cdd:cd07830  145 LARE 148
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
46-312 4.59e-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: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLG--QSEGVpqVYYFGPCGKYNALVLEL- 122
Cdd:cd13996    7 DFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAklNHPNI--VRYYTAWVEEPPLYIQMe 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 --LGPSLEDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsAKKQHIIYIIDFGLAKEYID 198
Cdd:cd13996   85 lcEGGTLRDWIDRRNSssKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL----DNDDLQVKIGDFGLATSIGN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 199 PETHKHIP-------YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFLRgslpwqglkaDTLKERYQKIG 269
Cdd:cd13996  161 QKRELNNLnnnnngnTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILfeMLHPF----------KTAMERSTILT 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 919096895 270 DTKRATPIEVLCENFPEElATYLRYVRRLDFFETPD-YDYLRKL 312
Cdd:cd13996  231 DLRNGILPESFKAKHPKE-ADLIQSLLSKNPEERPSaEQLLRSL 273
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
48-208 6.05e-12

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: 65.65  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895    48 RVGKKIGCGNFGELRLGKnLYNNEH-----VAIKLepMKSRAPQLHLEyRFYKQ---------------LGQSEGVPQVY 107
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGT-LKGKGDgkeveVAVKT--LKEDASEQQIE-EFLREarimrkldhpnivklLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   108 yfgpcgkynaLVLELL-GPSLED-LFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHII 185
Cdd:smart00221  78 ----------IVMEYMpGGDLLDyLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG-----ENLVV 142
                          170       180
                   ....*....|....*....|....*...
gi 919096895   186 YIIDFGLAKE-----YIDPETHKhIPYR 208
Cdd:smart00221 143 KISDFGLSRDlydddYYKVKGGK-LPIR 169
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
43-293 9.24e-12

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: 65.03  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  43 VGPNFrvgkkIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAP-QLHLEYRF-YKQLGQSEGV----PQVYYFGPCGKYN 116
Cdd:cd13995    7 IGSDF-----IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPsDVEIQACFrHENIAELYGAllweETVHLFMEAGEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALV--LELLGPSledlfdlcdRKFSlktVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKqhiiYIIDFGLAK 194
Cdd:cd13995   82 SVLekLESCGPM---------REFE---IIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF--MSTKA----VLVDFGLSV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 195 EYIDpetHKHIPyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIgDTKRA 274
Cdd:cd13995  144 QMTE---DVYVP----KDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYI-IHKQA 215
                        250
                 ....*....|....*....
gi 919096895 275 TPIevlcENFPEELATYLR 293
Cdd:cd13995  216 PPL----EDIAQDCSPAMR 230
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
47-253 1.20e-11

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: 64.66  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAP----QLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLEL 122
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcpeNIKKEVCIQKML-SHKNVVRFYGHRREGEFQYLFLEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LgpSLEDLFDLCD---------RKFSLKtvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd14069   82 A--SGGELFDKIEpdvgmpedvAQFYFQ-------QLMAGLKYLHSCGITHRDIKPENLLLDENDNLK-----ISDFGLA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 194 KEYI--DPEthkhipyREHKSLTGTARYMSINThLGKEQSRRD--DLEALGHMFMYFLRGSLPW 253
Cdd:cd14069  148 TVFRykGKE-------RLLNKMCGTLPYVAPEL-LAKKKYRAEpvDVWSCGIVLFAMLAGELPW 203
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
43-195 1.72e-11

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: 64.83  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  43 VGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPM----KSRAPQ----------LHLEYRFYKQLGQSEgvpQVYY 108
Cdd:cd14137    2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQdkryKNRELQimrrlkhpniVKLKYFFYSSGEKKD---EVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 109 FgpcgkynaLVLELLGPSLEDL---FDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHII 185
Cdd:cd14137   79 N--------LVMEYMPETLYRVirhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPET----GVL 146
                        170
                 ....*....|
gi 919096895 186 YIIDFGLAKE 195
Cdd:cd14137  147 KLCDFGSAKR 156
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
44-212 1.89e-11

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: 64.20  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  44 GPnFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEP----MKSRAPQ-LHLEYRFYKqLGQSEGVPQVYYFGPCGKYNAL 118
Cdd:cd14081    1 GP-YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNkeklSKESVLMkVEREIAIMK-LIEHPNVLKLYDVYENKKYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLgpSLEDLFD-LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK-- 194
Cdd:cd14081   79 VLEYV--SGGELFDyLVKKgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL-----DEKNNIKIADFGMASlq 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 919096895 195 -------------EYIDPETHKHIPYREHKS 212
Cdd:cd14081  152 pegslletscgspHYACPEVIKGEKYDGRKA 182
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
46-221 3.10e-11

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: 63.51  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK----LEPMKSRAPQLHL-EYRFYKQLGQSEGVPQVYYFGPCGKYNaLVL 120
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqiFEMMDAKARQDCVkEIDLLKQLNHPNVIKYLDSFIEDNELN-IVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELlgPSLEDL------FDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAK 194
Cdd:cd08228   82 EL--ADAGDLsqmikyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLGR 154
                        170       180
                 ....*....|....*....|....*..
gi 919096895 195 EYIDPETHKHipyrehkSLTGTARYMS 221
Cdd:cd08228  155 FFSSKTTAAH-------SLVGTPYYMS 174
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
46-268 7.39e-11

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: 62.81  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFY-KQLGQSEGVPQVYYFGPCGKYNA---LVLE 121
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNeKRILQAINFPFLVKLEYSFKDNSnlyMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLGPSleDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEyIDP 199
Cdd:cd14209   82 YVPGG--EMFSHLRRigRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI-----DQQGYIKVTDFGFAKR-VKG 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 200 ETHkhipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 268
Cdd:cd14209  154 RTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKI 210
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
47-199 9.36e-11

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: 62.27  E-value: 9.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEYRFYKQLGQSEGVP--QVYyfgPCGKYNALVLE 121
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIidkSKLKGKEDMIESEILIIKSLSHPNIVKlfEVY---ETEKEIYLILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLGPSleDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqSAKKQHIIYIIDFGLAKEYIDP 199
Cdd:cd14185   79 YVRGG--DLFDAIIEsvKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQH-NPDKSTTLKLADFGLAKYVTGP 155
pknD PRK13184
serine/threonine-protein kinase PknD;
137-291 1.23e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 63.64  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAK-------EYIDPETHKhiPYRE 209
Cdd:PRK13184 109 KTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGE-----VVILDWGAAIfkkleeeDLLDIDVDE--RNIC 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 210 HKSLT------GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkadtlKERYQKIGDTKRATPievlcen 283
Cdd:PRK13184 182 YSSMTipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR-------RKKGRKISYRDVILS------- 247

                 ....*...
gi 919096895 284 fPEELATY 291
Cdd:PRK13184 248 -PIEVAPY 254
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
47-212 1.76e-10

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: 61.52  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRAPQLH--LEYRFYKQLGQSEGVP------QVYYFGPCGKYnAL 118
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKC--MKKHFKSLEqvNNLREIQALRRLSPHPnilrliEVLFDRKTGRL-AL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGPSLEDLFDlcDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsakKQHIIYIIDFGLAKey 196
Cdd:cd07831   78 VFELMDMNLYELIK--GRKrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI------KDDILKLADFGSCR-- 147
                        170
                 ....*....|....*.
gi 919096895 197 idpETHKHIPYREHKS 212
Cdd:cd07831  148 ---GIYSKPPYTEYIS 160
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
46-193 2.14e-10

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: 60.86  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRA-----PQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd14078    4 YYELHETIGSGGFAKVKLATHILTGEKVAIKI--MDKKAlgddlPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 121 ELLgPSLEdLFDLCDRKFSLKT--VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLA 193
Cdd:cd14078   81 EYC-PGGE-LFDYIVAKDRLSEdeARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL-----DEDQNLKLIDFGLC 148
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
118-278 2.68e-10

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: 60.64  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL--GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI-GRQSAKkqhiiyIIDFGLAK 194
Cdd:cd14008   83 LVLEYCegGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLtADGTVK------ISDFGVSE 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 195 EYIDPEThkhipyrEHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKIGDT 271
Cdd:cd14008  157 MFEDGND-------TLQKTAGTPAFLApelCDGDSKTYSGKAADIWALGVTLYCLVFGRLPF---NGDNILELYEAIQNQ 226

                 ....*..
gi 919096895 272 KRATPIE 278
Cdd:cd14008  227 NDEFPIP 233
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
47-193 2.83e-10

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: 61.50  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRAP---QLHLEYRFYKQLGQsegvpqvyYFGPCGKYN------- 116
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKV--LKNKPAyfrQAMLEIAILTLLNT--------KYDPEDKHHivrlldh 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 -------ALVLELLGPSLEDLfdLCDRKF---SLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIY 186
Cdd:cd14212   71 fmhhghlCIVFELLGVNLYEL--LKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPE---IK 145

                 ....*..
gi 919096895 187 IIDFGLA 193
Cdd:cd14212  146 LIDFGSA 152
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
88-276 4.23e-10

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: 60.88  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  88 HLEYRFykqlgQSEGvpQVYyfgpcgkynaLVLELL-GPSL------EDLFDLCDRKFSLKtvlmiaiQLVTRMEYVHSK 160
Cdd:cd05582   61 KLHYAF-----QTEG--KLY----------LILDFLrGGDLftrlskEVMFTEEDVKFYLA-------ELALALDHLHSL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 161 HLIYRDVKPENFLIgrqsAKKQHiIYIIDFGLAKEYIDPETHKHipyrehkSLTGTARYMS---INTHlGKEQSRrdDLE 237
Cdd:cd05582  117 GIIYRDLKPENILL----DEDGH-IKLTDFGLSKESIDHEKKAY-------SFCGTVEYMApevVNRR-GHTQSA--DWW 181
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 919096895 238 ALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGDTKRATP 276
Cdd:cd05582  182 SFGVLMFEMLTGSLPFQG---KDRKETMTMILKAKLGMP 217
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
45-255 4.91e-10

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: 60.10  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  45 PNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL-----EPMKSRAPQLHL-----EYRFYKQLGQSeGVPQVYYFGPCGK 114
Cdd:cd14084    6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIinkrkFTIGSRREINKPrnietEIEILKKLSHP-CIIKIEDFFDAED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELLGPSleDLFDLCDRKFSLK--TVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakKQHIIYIIDFGL 192
Cdd:cd14084   85 DYYIVLELMEGG--ELFDRVVSNKRLKeaICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQE--EECLIKITDFGL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 193 AKeyIDPETHKhipyreHKSLTGTARYMS--INTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14084  161 SK--ILGETSL------MKTLCGTPTYLApeVLRSFGTEGyTRAVDCWSLGVILFICLSGYPPFSE 218
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
46-240 4.98e-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: 59.96  E-value: 4.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ----LHLEYRFYKQLGQSEGVPQVYYFGPCGKYNaLVLE 121
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKelrnLRQEIEILRKLNHPNIIEMLDSFETKKEFV-VVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LlgpSLEDLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEyIDP 199
Cdd:cd14002   81 Y---AQGELFQILedDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG-----KGGVVKLCDFGFARA-MSC 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 919096895 200 ETHKhipyreHKSLTGTARYMSinTHLGKEQ--SRRDDLEALG 240
Cdd:cd14002  152 NTLV------LTSIKGTPLYMA--PELVQEQpyDHTADLWSLG 186
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
47-199 6.59e-10

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: 59.65  E-value: 6.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQL----------HLEYRFYKQLGQSEGVPQVYYfgpcgky 115
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKiIDKAKCKGKEHmienevailrRVKHPNIVQLIEEYDTDTELY------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 116 naLVLELLgpSLEDLFD--LCDRKFSLK-TVLMIAiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGL 192
Cdd:cd14095   75 --LVMELV--KGGDLFDaiTSSTKFTERdASRMVT-DLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKS-LKLADFGL 148

                 ....*..
gi 919096895 193 AKEYIDP 199
Cdd:cd14095  149 ATEVKEP 155
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
106-268 7.55e-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: 60.11  E-value: 7.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 106 VYYFGPCGK-YnaLVLELLgpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkq 182
Cdd:cd05584   66 HYAFQTGGKlY--LILEYL--SGGELFMHLEREgiFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQG---- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 183 HIIyIIDFGLAKEYIDPETHKHipyrehkSLTGTARYMS--INTHLGkeQSRRDDLEALGHMfMY-FLRGSLPWQglkAD 259
Cdd:cd05584  138 HVK-LTDFGLCKESIHDGTVTH-------TFCGTIEYMApeILTRSG--HGKAVDWWSLGAL-MYdMLTGAPPFT---AE 203

                 ....*....
gi 919096895 260 TLKERYQKI 268
Cdd:cd05584  204 NRKKTIDKI 212
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
51-253 7.75e-10

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: 59.98  E-value: 7.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMKS---RAPQLH-----------LEYRFYKQLGQSEGVPQVYYFgpcgkyn 116
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTilkKKEQNHimaernvllknLKHPFLVGLHYSFQTSEKLYF------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 alVLELLGPSlEDLFDLC-DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKE 195
Cdd:cd05603   74 --VLDYVNGG-ELFFHLQrERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQG----HVV-LTDFGLCKE 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 196 YIDPETHKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05603  146 GMEPEETT-------STFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
46-268 7.83e-10

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: 59.49  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKS-----RAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAmqkagMVQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAkeyidp 199
Cdd:cd14186   81 EMChNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIK-----IADFGLA------ 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 200 eTHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 268
Cdd:cd14186  150 -TQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD---TDTVKNTLNKV 214
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
46-293 2.06e-09

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: 58.10  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKK--IGCGNFGELRLGKNLYNNE-HVAIKLEPMKSRAPQ---LHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALV 119
Cdd:cd14201    5 DFEYSRKdlVGHGAFAVVFKGRHRKKTDwEVAIKSINKKNLSKSqilLGKEIKILKEL-QHENIVALYDVQEMPNSVFLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLGPSleDLFDLCDRKFSLK--TVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHI----IYIIDFGLA 193
Cdd:cd14201   84 MEYCNGG--DLADYLQAKGTLSedTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVsgirIKIADFGFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 194 KeYIDPETHKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKigdTKR 273
Cdd:cd14201  162 R-YLQSNMMA-------ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEK---NKN 230
                        250       260
                 ....*....|....*....|
gi 919096895 274 ATPIevlcenFPEELATYLR 293
Cdd:cd14201  231 LQPS------IPRETSPYLA 244
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
37-221 2.25e-09

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: 58.48  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  37 GSGVLMvgpNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHL----EYRFYKQLGQSEGVP---QVYYF 109
Cdd:cd07866    3 GCSKLR---DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPItalrEIKILKKLKHPNVVPlidMAVER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 110 GPCGKYNALVLELLGPSLE-DLFDLCDR---KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhII 185
Cdd:cd07866   80 PDKSKRKRGSVYMVTPYMDhDLSGLLENpsvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG-----IL 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 919096895 186 YIIDFGLAKEYIDPethkhIPYREHKSLTGTARYMS 221
Cdd:cd07866  155 KIADFGLARPYDGP-----PPNPKGGGGGGTRKYTN 185
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
48-255 2.33e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.42  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  48 RVGKKIGCGNFGELRLGKNLYNNEHVAIKLepmksrapqLHLEY--------RFYKQlGQS------EGVPQVYYFGPCG 113
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKV---------LRPDLardpefvaRFRRE-AQSaaslshPNIVSVYDVGEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 KYNALVLELL-GPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGL 192
Cdd:NF033483  80 GIPYIVMEYVdGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVK-----VTDFGI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 193 AKEYidPEThkhipyrehkSLT------GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 255
Cdd:NF033483 154 ARAL--SST----------TMTqtnsvlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
46-221 3.09e-09

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: 57.67  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK----LEPM--KSRAPQLHlEYRFYKQLGQsegvPQVY-YFGPCGKYNAL 118
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKkvqiFEMMdaKARQDCLK-EIDLLQQLNH----PNIIkYLASFIENNEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 --VLELlgpslEDLFDLC---------DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyI 187
Cdd:cd08224   76 niVLEL-----ADAGDLSrlikhfkkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVK-----L 145
                        170       180       190
                 ....*....|....*....|....*....|....
gi 919096895 188 IDFGLAKeYIDPEThkhipyREHKSLTGTARYMS 221
Cdd:cd08224  146 GDLGLGR-FFSSKT------TAAHSLVGTPYYMS 172
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
56-254 3.94e-09

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: 57.14  E-value: 3.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  56 GNFGELRLGKNLYNNEHVAIKLEPM----KSRAPQlhlEYRFYKQLgQSEGVPQVY--YFGPcgKYNALVLELLGpSLED 129
Cdd:cd14111   14 GRFGVIRRCRENATGKNFPAKIVPYqaeeKQGVLQ---EYEILKSL-HHERIMALHeaYITP--RYLVLIAEFCS-GKEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYiDPETHKHIPYR 208
Cdd:cd14111   87 LHSLIDRfRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIK-----IVDFGSAQSF-NPLSLRQLGRR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 919096895 209 ehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14111  161 -----TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE 201
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
46-196 5.02e-09

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: 57.55  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRApqLHLEYRFYKQLGQSEGVPQVY--YFGPCGKYNALVLE- 121
Cdd:cd14132   19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKvLKPVKKKK--IKREIKILQNLRGGPNIVKLLdvVKDPQSKTPSLIFEy 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 -------LLGPSLEDLfdlcDRKFSLKtvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHIIYIIDFGLAK 194
Cdd:cd14132   97 vnntdfkTLYPTLTDY----DIRYYMY-------ELLKALDYCHSKGIMHRDVKPHNIMID----HEKRKLRLIDWGLAE 161

                 ..
gi 919096895 195 EY 196
Cdd:cd14132  162 FY 163
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
118-221 5.43e-09

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: 56.51  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFDLCDRKFSLkTVLMIAI---QLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHiIYIIDFGLAK 194
Cdd:cd14006   66 LILELC--SGGELLDRLAERGSL-SEEEVRTymrQLLEGLQYLHNHHILHLDLKPENILL--ADRPSPQ-IKIIDFGLAR 139
                         90       100
                 ....*....|....*....|....*..
gi 919096895 195 EyIDPETHKHipyrehkSLTGTARYMS 221
Cdd:cd14006  140 K-LNPGEELK-------EIFGTPEFVA 158
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
47-191 5.87e-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: 57.17  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRApQLH----LEYRFYKQLGQSEgvpqvyyfgPCGKYN------ 116
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKI--IRNKK-RFHqqalVEVKILKHLNDND---------PDDKHNivrykd 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 --------ALVLELLGPSLEDLfdLCDRKF---SLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgRQSAKKQhiI 185
Cdd:cd14210   83 sfifrghlCIVFELLSINLYEL--LKSNNFqglSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKSS--I 157

                 ....*.
gi 919096895 186 YIIDFG 191
Cdd:cd14210  158 KVIDFG 163
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
47-213 1.01e-08

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: 56.43  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRapqlhleyRFYKQLGQSE------------------GVPQVY- 107
Cdd:cd14136   12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKV--VKSA--------QHYTEAALDEikllkcvreadpkdpgreHVVQLLd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 108 YF---GPCGKYNALVLELLGPSLEDLFDLCD-RKFSLKTVLMIAIQLVTRMEYVHSK-HLIYRDVKPENFLIgrqsAKKQ 182
Cdd:cd14136   82 DFkhtGPNGTHVCMVFEVLGPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLL----CISK 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 919096895 183 HIIYIIDFGLAKeyidpETHKH----IPYREHKSL 213
Cdd:cd14136  158 IEVKIADLGNAC-----WTDKHftedIQTRQYRSP 187
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
149-268 1.04e-08

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: 56.07  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKE-YIDPETHKHI-------PYREHKSLTGTARYM 220
Cdd:cd05579  101 EIVLALEYLHSHGIIHRDLKPDNILIDANG-----HLKLTDFGLSKVgLVRRQIKLSIqkksngaPEKEDRRIVGTPDYL 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 221 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd05579  176 APEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHA---ETPEEIFQNI 220
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
135-287 1.07e-08

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: 56.04  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSlkTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGL--AKEYIDPETHKHIP---YRE 209
Cdd:cd14048  114 SRELF--VCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDD-----VVKVGDFGLvtAMDQGEPEQTVLTPmpaYAK 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 210 HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLrgslpwqgLKADTLKERYQKIGDTKRATPIEVLCENFPEE 287
Cdd:cd14048  187 HTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI--------YSFSTQMERIRTLTDVRKLKFPALFTNKYPEE 256
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
49-196 1.20e-08

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: 55.95  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKNLYNNEH-----VAIKL-----EPMKSRAPQLHLEYRFYKQLGQSEGVpQVYYFGPCGKYNAL 118
Cdd:cd14076    5 LGRTLGEGEFGKVKLGWPLPKANHrsgvqVAIKLirrdtQQENCQTSKIMREINILKGLTHPNIV-RLLDVLKTKKYIGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGPSleDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEY 196
Cdd:cd14076   84 VLEFVSGG--ELFDyiLARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-----DKNRNLVITDFGFANTF 156
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
118-201 1.25e-08

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: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSleDLFD-LCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqHIIYIIDFGLAK 194
Cdd:cd14103   67 LVMEYVAGG--ELFErVVDDDFELteRDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTG---NQIKIIDFGLAR 141

                 ....*..
gi 919096895 195 EYiDPET 201
Cdd:cd14103  142 KY-DPDK 147
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
52-194 1.28e-08

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: 56.17  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIKlePMKSRAPQLHL------EYRFYKQLGQSEGVPQVYYFGPCGKYNaLVLELLGP 125
Cdd:cd07833    8 VVGEGAYGVVLKCRNKATGEIVAIK--KFKESEDDEDVkktalrEVKVLRQLRHENIVNLKEAFRRKGRLY-LVFEYVER 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 126 SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd07833   85 TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLK-----LCDFGFAR 148
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
146-264 1.31e-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: 55.56  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhIIYIIDFGLAKeYIDPETHKhipyrehKSLTGTARYMSINTH 225
Cdd:cd14098  106 LTKQILEAMAYTHSMGITHRDLKPENILITQDDPV---IVKISDFGLAK-VIHTGTFL-------VTFCGTMAYLAPEIL 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 919096895 226 LGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKER 264
Cdd:cd14098  175 MSKEQNLQGgysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKR 219
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
118-268 1.42e-08

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: 55.76  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLEL-LGPSLEDLFDLcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiiyiiDFGLAKEY 196
Cdd:cd14010   71 LVVEYcTGGDLETLLRQ-DGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLS-----DFGLARRE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 ID---------PETHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFlrGSLPWQglkADTLKERY 265
Cdd:cd14010  145 GEilkelfgqfSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLyeMFT--GKPPFV---AESFTELV 219

                 ...
gi 919096895 266 QKI 268
Cdd:cd14010  220 EKI 222
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
50-198 1.51e-08

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 55.32  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIK-----LEP-MKSRAPQlhlEYRFYKQLGQSEGVPQVyyfGPCGKYNAL--VLE 121
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADNTPVAVKscretLPPdLKAKFLQ---EARILKQYSHPNIVRLI---GVCTQKQPIyiVME 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 122 LL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYID 198
Cdd:cd05084   75 LVqGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLK-----ISDFGMSREEED 147
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
51-267 1.52e-08

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 55.62  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGK---NLYNNEHVAIKLepMKSRAP-----QLHLEYRFYKQLGQsegvpqvyyfgPCgkynalVLEL 122
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKT--LKEDASeserkDFLKEARVMKKLGH-----------PN------VVRL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LGPSLED-----LFDLCDR--------------------KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrq 177
Cdd:cd00192   62 LGVCTEEeplylVMEYMEGgdlldflrksrpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVG-- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 178 sakKQHIIYIIDFGLAKeyidpethKHIPYREHKSLTGTA---RYM---SINTHLGKEQSrrdDLEALGhMFMY--FLRG 249
Cdd:cd00192  140 ---EDLVVKISDFGLSR--------DIYDDDYYRKKTGGKlpiRWMapeSLKDGIFTSKS---DVWSFG-VLLWeiFTLG 204
                        250
                 ....*....|....*...
gi 919096895 250 SLPWQGLKADTLKERYQK 267
Cdd:cd00192  205 ATPYPGLSNEEVLEYLRK 222
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
47-269 1.52e-08

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: 55.49  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL--------EPMKSrapQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNaL 118
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIidkeqvarEGMVE---QIKREIAIMKLLRHPNIVELHEVMATKTKIF-F 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGPSleDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA--K 194
Cdd:cd14663   78 VMELVTGG--ELFSkiAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLK-----ISDFGLSalS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 195 EYIDPETHKHipyrehkSLTGTARYMSinthlgKEQSRRD-------DLEALGHMFMYFLRGSLPWQglkADTLKERYQK 267
Cdd:cd14663  151 EQFRQDGLLH-------TTCGTPNYVA------PEVLARRgydgakaDIWSCGVILFVLLAGYLPFD---DENLMALYRK 214

                 ..
gi 919096895 268 IG 269
Cdd:cd14663  215 IM 216
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
51-194 1.52e-08

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: 55.85  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGK--NLYNN--EHVAIK-LEPMKSRAPQ--LHLEYRFYKQLgQSEGVpqVYYFGPC----GKYNALV 119
Cdd:cd05038   10 KQLGEGHFGSVELCRydPLGDNtgEQVAVKsLQPSGEEQHMsdFKREIEILRTL-DHEYI--VKYKGVCespgRRSLRLI 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 120 LELLgP--SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK 194
Cdd:cd05038   87 MEYL-PsgSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILV-----ESEDLVKISDFGLAK 157
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
47-272 1.74e-08

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: 55.80  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEyrFYKQLGQSEGVPQVYYFGPCGKYNALVLELL-GP 125
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIE--ILLRYGQHPNIITLKDVYDDGKHVYLVTELMrGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAKEyidpethkhi 205
Cdd:cd14175   81 ELLDKI-LRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPES-LRICDFGFAKQ---------- 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 206 pYREHKSLTGTARYMS--INTHLGKEQSRRD--DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 272
Cdd:cd14175  149 -LRAENGLLMTPCYTAnfVAPEVLKRQGYDEgcDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGK 218
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
47-252 1.87e-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: 55.29  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKQLgQSEGVpqVYYFGP--CGKYNALVLELL 123
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIInEILIMKEC-KHPNI--VDYYDSylVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEyIDPETH 202
Cdd:cd06614   79 dGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLS-----KDGSVKLADFGFAAQ-LTKEKS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06614  153 K------RNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
51-219 1.96e-08

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 55.59  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRAPQLHL-EYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLGPS 126
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNETIAlkkIRLEQEDEGVPSTAIrEISLLKEM-QHGNIVRLQDVVHSEKRLYLVFEYLDLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLC-DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIYIIDFGLAKEY-IDPETHKH 204
Cdd:PLN00009  87 LKKHMDSSpDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRT----NALKLADFGLARAFgIPVRTFTH 162
                        170
                 ....*....|....*....
gi 919096895 205 ----IPYREHKSLTGTARY 219
Cdd:PLN00009 163 evvtLWYRAPEILLGSRHY 181
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
46-220 1.98e-08

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: 55.08  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGEL-----RLGKNLYNNEHVAIKLEPMKSRAPQLHlEYRFYKQLGQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd13997    1 HFHELEQIGSGSFSEVfkvrsKVDGCLYAVKKSKKPFRGPKERARALR-EVEAHAALGQHPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL-GPSLEDLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeyi 197
Cdd:cd13997   80 ELCeNGSLQDALEELspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCK-----IGDFGLAT--- 151
                        170       180
                 ....*....|....*....|...
gi 919096895 198 dpETHKHIPYREhksltGTARYM 220
Cdd:cd13997  152 --RLETSGDVEE-----GDSRYL 167
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
45-196 2.11e-08

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: 54.92  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  45 PNFRVGKKIGCGNF-----GELRLGKNLYN--NEHVAIKlEPMKSRAPQLHL-EYRFYKQLGQSEGVPQVYYfgpCGKYN 116
Cdd:cd14019    1 NKYRIIEKIGEGTFssvykAEDKLHDLYDRnkGRLVALK-HIYPTSSPSRILnELECLERLGGSNNVSGLIT---AFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLgPSLE-----DLFdlcdRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiYIIDFG 191
Cdd:cd14019   77 DQVVAVL-PYIEhddfrDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKG----VLVDFG 147

                 ....*
gi 919096895 192 LAKEY 196
Cdd:cd14019  148 LAQRE 152
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
47-274 2.17e-08

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: 55.41  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFykQLGQSEGVPQVYYFGPCGKYNALVLELL-GP 125
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILL--RYGQHPNIITLKDVYDDGKFVYLVMELMrGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAKEyidpethkhi 205
Cdd:cd14178   83 ELLDRI-LRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPES-IRICDFGFAKQ---------- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 206 pYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRA 274
Cdd:cd14178  151 -LRAENGLLMTPCYTA--NFVAPEVLKRQgydaacDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYA 222
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
133-221 2.22e-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: 55.09  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 133 LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKEYIDPEThkhipYREHk 211
Cdd:cd05583   90 LYQReHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEG----HVV-LTDFGLSKEFLPGEN-----DRAY- 158
                         90
                 ....*....|
gi 919096895 212 SLTGTARYMS 221
Cdd:cd05583  159 SFCGTIEYMA 168
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
46-268 2.62e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 55.21  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQlHL--EYRFYKQLGQSEGVPQVYYFGPCGKYNALV 119
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKClkkrEILKMKQVQ-HVaqEKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLGpslEDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyi 197
Cdd:PTZ00263  98 EFVVG---GELFTHLRKagRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVK-----VTDFGFAKK-- 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 198 dpethkhIPYREHkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:PTZ00263 168 -------VPDRTF-TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFD---DTPFRIYEKI 227
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
46-253 2.94e-08

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: 54.67  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAP----QLHLEYRFYKQLgQSEGVpqVYYFGpCGKYN-- 116
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKqveIDPINTEASkevkALECEIQLLKNL-QHERI--VQYYG-CLQDEks 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 -ALVLELL-GPSLED-------LFDLCDRKFSLktvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLigRQSAKKqhiIYI 187
Cdd:cd06625   77 lSIFMEYMpGGSVKDeikaygaLTENVTRKYTR--------QILEGLAYLHSNMIVHRDIKGANIL--RDSNGN---VKL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 188 IDFGLAKEYIDPETHKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06625  144 GDFGASKRLQTICSSTGM-----KSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW 204
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
46-240 3.01e-08

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: 54.65  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL-----EPmksRAPQLHLEYRFYKQLGQSEGVPQVY----YFGPCGKYN 116
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRmyfndEE---QLRVAIKEIEIMKRLCGHPNIVQYYdsaiLSSEGRKEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSLEDLFDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKH--LIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd13985   78 LLLMEYCPGSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFK-----LCDFGSA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 919096895 194 -KEYIDPETHKHIPYRE-----HKSLTGTARYMsINTHLGKEQSRRDDLEALG 240
Cdd:cd13985  153 tTEHYPLERAEEVNIIEeeiqkNTTPMYRAPEM-IDLYSKKPIGEKADIWALG 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
52-203 3.02e-08

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: 55.07  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL-EYRFYKQLGQSEGVP--QVYYfGPCGKYNA------LV 119
Cdd:cd07865   19 KIGQGTFGEVFKARHRKTGQIVALKkvlMENEKEGFPITALrEIKILQLLKHENVVNliEICR-TKATPYNRykgsiyLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYIDP 199
Cdd:cd07865   98 FEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG-----VLKLADFGLARAFSLA 172

                 ....
gi 919096895 200 ETHK 203
Cdd:cd07865  173 KNSQ 176
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
135-253 3.46e-08

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: 55.01  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHiIYIIDFGLAKEYIDPEThkhipyrEHKSLT 214
Cdd:cd05595   89 ERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD----KDGH-IKITDFGLCKEGITDGA-------TMKTFC 156
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 919096895 215 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05595  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
118-291 3.47e-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: 54.62  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyi 197
Cdd:cd07873   77 LVFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELK-----LADFGLARA-- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 198 dpethKHIPYREHKSLTGTARYMSINTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGDTkRATP 276
Cdd:cd07873  150 -----KSIPTKTYSNEVVTLWYRPPDILLGStDYSTQIDMWGVGCIFYEMSTGRPLFPG---STVEEQLHFIFRI-LGTP 220
                        170       180
                 ....*....|....*....|
gi 919096895 277 IEvlcENFP-----EELATY 291
Cdd:cd07873  221 TE---ETWPgilsnEEFKSY 237
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
51-320 3.69e-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: 54.97  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMK---SRAPQLHLEYR---FYKQLGQSEGVPQVYYFGPCGKYnALVLELLG 124
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAErnvLLKNVKHPFLVGLHYSFQTTDKL-YFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSlEDLFDLC-DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKEYI---DPE 200
Cdd:cd05604   81 GG-ELFFHLQrERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQG----HIV-LTDFGLCKEGIsnsDTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 201 ThkhipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL------KERYQKIGDTKRA 274
Cdd:cd05604  155 T----------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMyenilhKPLVLRPGISLTA 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 275 TPI-EVLCENFPEelatyLRYVRRLDFFETPDYDYLRKL-FTDLMAKK 320
Cdd:cd05604  225 WSIlEELLEKDRQ-----LRLGAKEDFLEIKNHPFFESInWTDLVQKK 267
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
46-221 4.01e-08

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: 54.01  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL-EYRFYKQLGQsegvPQV--YY----------- 108
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeidLSNMSEKEREEALnEVKLLSKLKH----PNIvkYYesfeengklci 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 109 ---FGPCGkynalvlellgpsleDLFDL------CDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPEN-FLigrqs 178
Cdd:cd08215   77 vmeYADGG---------------DLAQKikkqkkKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNiFL----- 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 919096895 179 aKKQHIIYIIDFGLAKEYIDPETHKhipyrehKSLTGTARYMS 221
Cdd:cd08215  137 -TKDGVVKLGDFGISKVLESTTDLA-------KTVVGTPYYLS 171
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
47-268 4.29e-08

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: 54.10  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEP----MKSRAPQ-LHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPksslTKPKQREkLKSEIKIHRSL-KHPNIVKFHDCFEDEENVYILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLgpSLEDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyIDP 199
Cdd:cd14099   82 LC--SNGSLMELLKRrkALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVK-----IGDFGLAAR-LEY 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 200 ETHKhipyreHKSLTGTARYMS--InthLGKEQ--SRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 268
Cdd:cd14099  154 DGER------KKTLCGTPNYIApeV---LEKKKghSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRI 214
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
48-252 5.22e-08

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 54.03  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  48 RVGKKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVY-------YFGPCGKYNAL 118
Cdd:cd13975    3 KLGRELGRGQYGVVYACDSWGGHFPCALKsvVPPDDKHWNDLALEFHYTRSLPKHERIVSLHgsvidysYGGGSSIAVLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGpslEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeyid 198
Cdd:cd13975   83 IMERLH---RDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAK-----ITDLGFCK---- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 199 PETHKhipyreHKSLTGTARYMSINTHLGKEQSRRdDLEALGHMFMYFLRGS--LP 252
Cdd:cd13975  151 PEAMM------SGSIVGTPIHMAPELFSGKYDNSV-DVYAFGILFWYLCAGHvkLP 199
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
50-200 5.54e-08

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: 53.61  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLyNNEHVAIKL--EPMKSRAPQLHlEYRFYKQLgQSEGVPQVYyfGPCGKYNAL--VLELLG- 124
Cdd:cd05059    9 LKELGSGQFGVVHLGKWR-GKIDVAIKMikEGSMSEDDFIE-EAKVMMKL-SHPKLVQLY--GVCTKQRPIfiVTEYMAn 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 125 PSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEYIDPE 200
Cdd:cd05059   84 GCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG-----EQNVVKVSDFGLARYVLDDE 154
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
135-255 5.67e-08

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: 53.80  E-value: 5.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAkeyidpeTHKHiPYREHKSLT 214
Cdd:cd05578   94 KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQG----H-VHITDFNIA-------TKLT-DGTLATSTS 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 919096895 215 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd05578  161 GTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEI 201
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
46-253 5.94e-08

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: 53.85  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLynNEHVAIKLEPMK-----------SRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGK 114
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKV--SGHDAGKLYAMKvlkkativqkaKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELLGPSleDLFD-LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGL 192
Cdd:cd05613   79 KLHLILDYINGG--ELFThLSQReRFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSG----HVV-LTDFGL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 193 AKEYIDPETHKHIpyrehkSLTGTARYMSINTHLGKE--QSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05613  152 SKEFLLDENERAY------SFCGTIEYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLTGASPF 208
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
111-267 6.19e-08

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: 53.85  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 111 PCGKYnALVLELLgpSLEDLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYII 188
Cdd:cd13994   69 LHGKW-CLVMEYC--PGGDLFTLIekADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDE-----DGVLKLT 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 189 DFGLAKEYIDPEtHKHIPYRehKSLTGTARYMSINTHLGKEQS-RRDDLEALGHMFMYFLRGSLPWQglKADTLKERYQK 267
Cdd:cd13994  141 DFGTAEVFGMPA-EKESPMS--AGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWR--SAKKSDSAYKA 215
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
46-208 6.88e-08

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: 53.73  E-value: 6.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL----EYRFYKQLGQSEGVPQVYYFGPCGKYNaL 118
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKkikLGERKEAKDGINFtalrEIKLLQELKHPNIIGLLDVFGHKSNIN-L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGPSLEDLFDlcDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEY 196
Cdd:cd07841   80 VFEFMETDLEKVIK--DKSivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA-----SDGVLKLADFGLARSF 152
                        170
                 ....*....|....*..
gi 919096895 197 IDPE---THKHIP--YR 208
Cdd:cd07841  153 GSPNrkmTHQVVTrwYR 169
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
118-292 7.18e-08

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: 53.86  E-value: 7.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyi 197
Cdd:cd07871   80 LVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELK-----LADFGLARA-- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 198 dpethKHIPYREHKSLTGTARYMSINTHLGK-EQSRRDDLEALG--HMFMYFLRGSLPwqglkADTLKERYQKIGDTkRA 274
Cdd:cd07871  153 -----KSVPTKTYSNEVVTLWYRPPDVLLGStEYSTPIDMWGVGciLYEMATGRPMFP-----GSTVKEELHLIFRL-LG 221
                        170       180
                 ....*....|....*....|...
gi 919096895 275 TPIEvlcENFP-----EELATYL 292
Cdd:cd07871  222 TPTE---ETWPgvtsnEEFRSYL 241
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
156-201 7.20e-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: 53.86  E-value: 7.20e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 919096895 156 YVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKEYIDPET 201
Cdd:cd05575  111 YLHSLNIIYRDLKPENILLDSQG----HVV-LTDFGLCKEGIEPSD 151
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-194 7.60e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 54.27  E-value: 7.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  29 HSNRTSSSGSGVLMV------GPN--FRVGKKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSRAPQL-------HLEY 91
Cdd:PTZ00036  42 HNNNAGEDEDEEKMIdndinrSPNksYKLGNIIGNGSFGVVYEAICIDTSEKVAIKkvLQDPQYKNRELlimknlnHINI 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  92 RFYKQlgqsegvpqvYYFGPCGKYNA------LVLELLGPSLEDLFDLCDRK---FSLKTVLMIAIQLVTRMEYVHSKHL 162
Cdd:PTZ00036 122 IFLKD----------YYYTECFKKNEkniflnVVMEFIPQTVHKYMKHYARNnhaLPLFLVKLYSYQLCRALAYIHSKFI 191
                        170       180       190
                 ....*....|....*....|....*....|..
gi 919096895 163 IYRDVKPENFLIgrqsAKKQHIIYIIDFGLAK 194
Cdd:PTZ00036 192 CHRDLKPQNLLI----DPNTHTLKLCDFGSAK 219
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
51-209 7.70e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 53.75  E-value: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNN----EHVAIKlePMKSRAPQLHL-----EYRFYKQLGQSEgvpQVYYFGPC----GKYNA 117
Cdd:cd05080   10 RDLGEGHFGKVSLYCYDPTNdgtgEMVAVK--ALKADCGPQHRsgwkqEIDILKTLYHEN---IVKYKGCCseqgGKSLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFD-LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDFGLAKEY 196
Cdd:cd05080   85 LIMEYV--PLGSLRDyLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN-----DRLVKIGDFGLAKAV 157
                        170
                 ....*....|...
gi 919096895 197 idPETHKHIPYRE 209
Cdd:cd05080  158 --PEGHEYYRVRE 168
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
51-194 8.13e-08

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 53.06  E-value: 8.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKnlYNNE-HVAIK-LEPmKSRAPQLHL-EYRFYKQLgQSEGVPQVYyfGPCGK----YnaLVLELL 123
Cdd:cd05034    1 KKLGAGQFGEVWMGV--WNGTtKVAVKtLKP-GTMSPEAFLqEAQIMKKL-RHDKLVQLY--AVCSDeepiY--IVTELM 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 124 --GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd05034   73 skGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCK-----VADFGLAR 140
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
50-221 8.47e-08

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: 53.18  E-value: 8.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIK-----LEPMKSR--APQLHLEYRFYKQLgQSEGVpqVYYFGPCGKYNAL--VL 120
Cdd:cd06632    5 GQLLGSGSFGSVYEGFNGDTGDFFAVKevslvDDDKKSResVKQLEQEIALLSKL-RHPNI--VQYYGTEREEDNLyiFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL-GPSLEDLFdlcdRKF-SLKTVLmiaIQLVTR-----MEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd06632   82 EYVpGGSIHKLL----QRYgAFEEPV---IRLYTRqilsgLAYLHSRNTVHRDIKGANILVDTNGVVK-----LADFGMA 149
                        170       180
                 ....*....|....*....|....*....
gi 919096895 194 keyidpethKHIPYREH-KSLTGTARYMS 221
Cdd:cd06632  150 ---------KHVEAFSFaKSFKGSPYWMA 169
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
118-268 8.74e-08

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: 53.26  E-value: 8.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFDLCDRKFSLKTVLMIAI--QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAke 195
Cdd:cd14105   85 LILELV--AGGELFDFLAEKESLSEEEATEFlkQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPR-IKLIDFGLA-- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 196 yidpetHKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd14105  160 ------HKIEDGNEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLG---DTKQETLANI 223
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
39-193 8.83e-08

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 52.72  E-value: 8.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  39 GVLMVGPNFRVGKKIGCGNFGELRLGKnlYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPcgkyNAL 118
Cdd:COG2112   34 SIYSGGTLIGGLRLLGKGYRGVVFLGK--LGGKKVALKIRRTDSPRPSLKKEAEILKKANGAGVGPKLYDYGR----DFL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELL-GPSLEDlfdlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDV-KPENfligrqsakkqHII------YIIDF 190
Cdd:COG2112  108 VMEYIeGEPLKD----WLENLDKEELRKVIRELLEAAYLLDRIGIDHGELsRPGK-----------HVIvdkgrpYIIDF 172

                 ...
gi 919096895 191 GLA 193
Cdd:COG2112  173 ESA 175
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
118-254 9.75e-08

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: 53.51  E-value: 9.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSleDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQhiIYIIDFGLAKe 195
Cdd:cd14179   79 LVMELLKGG--ELLERIKKKqhFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE--IKIIDFGFAR- 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 196 yIDPETHKHIpyrehKSLTGTARYMS--INTHLGKEQSRrdDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14179  154 -LKPPDNQPL-----KTPCFTLHYAApeLLNYNGYDESC--DLWSLGVILYTMLSGQVPFQ 206
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
43-208 1.00e-07

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: 53.52  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  43 VGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQL----HLEYRFYKQLGQSEGVPQVYYFGPCGKYNA- 117
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTakrtLRELKILRHFKHDNIIAIRDILRPKVPYADf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 ----LVLELLGPSLEDLFDlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd07855   83 kdvyVVLDLMESDLHHIIH-SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELK-----IGDFGMA 156
                        170       180
                 ....*....|....*....|....
gi 919096895 194 KEYI-DPETHK-----HI---PYR 208
Cdd:cd07855  157 RGLCtSPEEHKyfmteYVatrWYR 180
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
147-268 1.04e-07

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: 53.88  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 147 AIQLVTRMEYVHskhliyRDVKPENFLIGrqsaKKQHiIYIIDFGLAKEYIDPE--------------------TH---- 202
Cdd:cd05600  123 AISSLHQLGYIH------RDLKPENFLID----SSGH-IKLTDFGLASGTLSPKkiesmkirleevkntaflelTAkerr 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 203 -------KHIPYREHkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd05600  192 niyramrKEDQNYAN-SVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG---STPNETWANL 260
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
53-220 1.16e-07

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: 52.61  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAP----QLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLgpSLE 128
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKklqeNLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYC--AGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKeYIDPETHKHip 206
Cdd:cd14009   78 DLSQYIRKRGRLpeAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLL--STSGDDPVLKIADFGFAR-SLQPASMAE-- 152
                        170
                 ....*....|....
gi 919096895 207 yrehkSLTGTARYM 220
Cdd:cd14009  153 -----TLCGSPLYM 161
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
106-240 1.27e-07

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: 52.52  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 106 VYYFGPCGKYNAL--VLELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgRQSAKKQ 182
Cdd:cd14156   51 VRYLGICVKDEKLhpILEYVsGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLI-RVTPRGR 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 183 HIIyIIDFGLAKEYIDPETHKhiPYREhKSLTGTARYMSINTHLGKEQSRRDDLEALG 240
Cdd:cd14156  130 EAV-VTDFGLAREVGEMPAND--PERK-LSLVGSAFWMAPEMLRGEPYDRKVDVFSFG 183
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
46-204 1.35e-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: 52.83  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPmksRAPQLHLEYRFYKQlGQSEGVPQVYYFgpcgKYNALVLELLGP 125
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIP---RASNAGLKKEREKR-LEKEISRDIRTI----REAALSSLLNHP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCD--------------------------------RKFslktvlmiAIQLVTRMEYVHSKHLIYRDVKPENFL 173
Cdd:cd14077   74 HICRLRDFLRtpnhyymlfeyvdggqlldyiishgklkekqaRKF--------ARQIASALDYLHRNSIVHRDLKIENIL 145
                        170       180       190
                 ....*....|....*....|....*....|.
gi 919096895 174 IGRQSAKKqhiiyIIDFGLAKEYiDPETHKH 204
Cdd:cd14077  146 ISKSGNIK-----IIDFGLSNLY-DPRRLLR 170
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
52-196 1.52e-07

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: 52.82  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL-EYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLGPSL 127
Cdd:cd07839    7 KIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEGVPSSALrEICLLKEL-KHKNIVRLYDVLHSDKKLTLVFEYCDQDL 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEY 196
Cdd:cd07839   86 KKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELK-----LADFGLARAF 149
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
47-268 1.77e-07

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: 52.44  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLyNNEHVAIKL--EPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL- 123
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKIlkSDDLLKQQDFQKEVQALKRL-RHKHLISLFAVCSVGEPVYIITELMe 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA---KEYIDP 199
Cdd:cd05148   86 kGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCK-----VADFGLArliKEDVYL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 200 ETHKHIPYRehksltGTARYMSINTHLgkeqSRRDDLEALGhMFMY--FLRGSLPWQGLkadTLKERYQKI 268
Cdd:cd05148  161 SSDKKIPYK------WTAPEAASHGTF----STKSDVWSFG-ILLYemFTYGQVPYPGM---NNHEVYDQI 217
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
46-221 1.86e-07

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: 52.34  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK------LEPMKSRAPQLHlEYRFYKQLGQSEGVPQVYYFGPCGKYNaLV 119
Cdd:cd08229   25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKkvqifdLMDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELN-IV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLGPSleDL------FDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLA 193
Cdd:cd08229  103 LELADAG--DLsrmikhFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLG 175
                        170       180
                 ....*....|....*....|....*...
gi 919096895 194 KEYIDPETHKHipyrehkSLTGTARYMS 221
Cdd:cd08229  176 RFFSSKTTAAH-------SLVGTPYYMS 196
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
51-208 1.94e-07

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: 51.97  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNE---HVAIKL---EPMKSRAPQLHLEYRFYKQLGQsegvPQ-VYYFGPC-GKYNALVLEL 122
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSGkevEVAVKTlkqEHEKAGKKEFLREASVMAQLDH----PCiVRLIGVCkGEPLMLVMEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 --LGPSLEDLFDlcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK------ 194
Cdd:cd05060   77 apLGPLLKYLKK--RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL-----VNRHQAKISDFGMSRalgags 149
                        170
                 ....*....|....
gi 919096895 195 EYIDPETHKHIPYR 208
Cdd:cd05060  150 DYYRATTAGRWPLK 163
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
53-316 2.10e-07

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: 51.91  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRlgKNLYNNEHVAIKL------EPMKSRAPQLHLEYRFYKQLGQsegvPQVYYF-GPCGK--YNALVLELL 123
Cdd:cd14148    2 IGVGGFGKVY--KGLWRGEEVAVKAarqdpdEDIAVTAENVRQEARLFWMLQH----PNIIALrGVCLNppHLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKH---LIYRDVKPENFLIGRQSAKKQ---HIIYIIDFGLAKEY 196
Cdd:cd14148   76 rGGALNRA--LAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIENDDlsgKTLKITDFGLAREW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 idpetHKhipyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDTKRATP 276
Cdd:cd14148  154 -----HK----TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR--EIDALAVAY-GVAMNKLTLP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 919096895 277 IEVLCenfPEELATYLRYVRRLDFFETPDYDYLRKLFTDL 316
Cdd:cd14148  222 IPSTC---PEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
53-313 2.21e-07

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: 52.74  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK--LEPMKS--RAPQLHLEYRFYKQLGQSEGVPQVYYFGPCG---KYNA--LVLELL 123
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKklSRPFQSliHARRTYRELRLLKHMKHENVIGLLDVFTPATsieNFNEvyLVTNLM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLcdRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEyIDPETHK 203
Cdd:cd07878  103 GADLNNIVKC--QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE-----LRILDFGLARQ-ADDEMTG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 204 HIPYREHKSLTGTARYMSINTHLgkeqsrrdDLEALGHMFMYFLRGSLPWQGLK-ADTLKERYQKIGdtkraTPIEVLCE 282
Cdd:cd07878  175 YVATRWYRAPEIMLNWMHYNQTV--------DIWSVGCIMAELLKGKALFPGNDyIDQLKRIMEVVG-----TPSPEVLK 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 919096895 283 NFPEELATylRYVRRLDFFETPDydyLRKLF 313
Cdd:cd07878  242 KISSEHAR--KYIQSLPHMPQQD---LKKIF 267
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
118-199 2.25e-07

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: 51.87  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLC-DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAkEY 196
Cdd:cd14119   73 MVMEYCVGGLQEMLDSApDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL-----TTDGTLKISDFGVA-EA 146

                 ...
gi 919096895 197 IDP 199
Cdd:cd14119  147 LDL 149
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
146-252 2.39e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 52.52  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKqhiIYIIDFGLAK---EYIDPethkhipyreHKSLTGTARYMS- 221
Cdd:PLN00034 173 VARQILSGIAYLHRRHIVHRDIKPSNLLI--NSAKN---VKIADFGVSRilaQTMDP----------CNSSVGTIAYMSp 237
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 919096895 222 --INTHL--GKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:PLN00034 238 erINTDLnhGAYDGYAGDIWSLGVSILEFYLGRFP 272
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
53-220 2.63e-07

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: 51.69  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLepMKSRAPQLHL------EYRFYKQLGQSEGVPQVYYF---GPCGkynaLVLELL 123
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKC--LHSSPNCIEErkallkEAEKMERARHSYVLPLLGVCverRSLG----LVMEYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLC--DRKFSLKtvLMIAIQLVTRMEYVH--SKHLIYRDVKPENFLIgrqsakKQHI-IYIIDFGLAKEYI 197
Cdd:cd13978   75 eNGSLKSLLEREiqDVPWSLR--FRIIHEIALGMNFLHnmDPPLLHHDLKPENILL------DNHFhVKISDFGLSKLGM 146
                        170       180
                 ....*....|....*....|...
gi 919096895 198 dpETHKHIPYREHKSLTGTARYM 220
Cdd:cd13978  147 --KSISANRRRGTENLGGTPIYM 167
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
47-272 2.68e-07

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: 52.33  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFykQLGQSEGVPQVYYFGPCGKYNALVLELL-GP 125
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILL--RYGQHPNIITLKDVYDDGKYVYVVTELMkGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAKEyidpethkhi 205
Cdd:cd14176   99 ELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPES-IRICDFGFAKQ---------- 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 206 pYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 272
Cdd:cd14176  167 -LRAENGLLMTPCYTA--NFVAPEVLERQgydaacDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGK 236
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
49-256 3.26e-07

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: 51.60  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKNlynNEHVAIKLEPMKSRAPQlhlEYRFYKQ----LGQSEGVPQVYYFGPCGKYN-ALVLELL 123
Cdd:cd14151   12 VGQRIGSGSFGTVYKGKW---HGDVAVKMLNVTAPTPQ---QLQAFKNevgvLRKTRHVNILLFMGYSTKPQlAIVTQWC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeyidpETH 202
Cdd:cd14151   86 eGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK-----IGDFGLAT-----VKS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 203 KHIPYREHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGL 256
Cdd:cd14151  156 RWSGSHQFEQLSGSILWMApevIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI 212
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
118-249 3.32e-07

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: 51.50  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDlcdRKFSLKTVLMIAIQLVTRME-------YVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDF 190
Cdd:cd13982   72 IALELCAASLQDLVE---SPRESKLFLRPGLEPVRLLRqiasglaHLHSLNIVHRDLKPQNILISTPNAHGNVRAMISDF 148
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 191 GLAKEyIDPETHKhipYREHKSLTGT----ARYMsINTHLGKEQSRRDDLEALGHMFMYFLRG 249
Cdd:cd13982  149 GLCKK-LDVGRSS---FSRRSGVAGTsgwiAPEM-LSGSTKRRQTRAVDIFSLGCVFYYVLSG 206
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
47-207 3.44e-07

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: 51.53  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQ----------------LHLEY--RFYKQLgqsEGVPQVYy 108
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVS-KKKAPEdylqkflpreievikgLKHPNliCFYEAI---ETTSRVY- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 109 fgpcgkynaLVLELL--GpsleDLFDLCDRKFSLKTVL--MIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHI 184
Cdd:cd14162   77 ---------IIMELAenG----DLLDYIRKNGALPEPQarRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD----KNNNL 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 919096895 185 IyIIDFGLAKE--------------------YIDPETHKHIPY 207
Cdd:cd14162  140 K-ITDFGFARGvmktkdgkpklsetycgsyaYASPEILRGIPY 181
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
46-268 3.45e-07

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: 51.40  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEpMKSRAPQLHLEYRFYKQLG-----QSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd14117    7 DFDIGRPLGKGKFGNVYLAREKQSKFIVALKVL-FKSQIEKEGVEHQLRREIEiqshlRHPNILRLYNYFHDRKRIYLIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL--GPSLEDLFDLCdrKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAkeyid 198
Cdd:cd14117   86 EYAprGELYKELQKHG--RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELK-----IADFGWS----- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 199 pethKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 268
Cdd:cd14117  154 ----VHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE---SASHTETYRRI 216
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
49-195 3.51e-07

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 51.20  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGknLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKQLGQSEGVPQVyyfGPCGKYNAL--VLELLGP 125
Cdd:cd05039   10 LGELIGKGEFGDVMLG--DYRGQKVAVKCLKDDSTAAQAFLaEASVMTTLRHPNLVQLL---GVVLEGNGLyiVTEYMAK 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 126 -SLEDLFDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd05039   85 gSLVDYLRSRGRAvITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAK-----VSDFGLAKE 151
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
51-263 3.71e-07

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: 51.87  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIK-----LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELL-G 124
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKalkkdVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLnG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSLedLFDLCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIdpethk 203
Cdd:cd05620   81 GDL--MFHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-----IKIADFGMCKENV------ 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 204 hipYREHKSLT--GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 263
Cdd:cd05620  148 ---FGDNRASTfcGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFE 206
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
147-253 3.77e-07

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: 51.94  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 147 AIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKEYIDPETHKhipyrehKSLTGTARYMSINTHL 226
Cdd:cd05602  114 AAEIASALGYLHSLNIVYRDLKPENILLDSQG----HIV-LTDFGLCKENIEPNGTT-------STFCGTPEYLAPEVLH 181
                         90       100
                 ....*....|....*....|....*..
gi 919096895 227 GKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05602  182 KQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
129-293 3.80e-07

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: 51.22  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRKFSLK--TVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQH----IIYIIDFGLAKeYIDPETH 202
Cdd:cd14120   78 DLADYLQAKGTLSedTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSpndiRLKIADFGFAR-FLQDGMM 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDtkratpievLCE 282
Cdd:cd14120  157 A-------ATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNAN---------LRP 220
                        170
                 ....*....|.
gi 919096895 283 NFPEELATYLR 293
Cdd:cd14120  221 NIPSGTSPALK 231
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
146-266 3.84e-07

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: 51.17  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYIIDFGLAKEYIDPETHKH--IPYREHKSLTgtaryMSIN 223
Cdd:cd13987   96 CAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRR---VKLCDFGLTRRVGSTVKRVSgtIPYTAPEVCE-----AKKN 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 919096895 224 THLGKEQSRrdDLEALGHMFMYFLRGSLPWQglKADTLKERYQ 266
Cdd:cd13987  168 EGFVVDPSI--DVWAFGVLLFCCLTGNFPWE--KADSDDQFYE 206
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
53-289 3.86e-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: 51.20  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGelRLGKNLYNNEHVAIKL------EPMKSRAPQLHLEYRFYKQLGQsegvPQVYYF-GPCGKYN--ALVLELL 123
Cdd:cd14145   14 IGIGGFG--KVYRAIWIGDEVAVKAarhdpdEDISQTIENVRQEAKLFAMLKH----PNIIALrGVCLKEPnlCLVMEFA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHL---IYRDVKPENFLIGRQSAK---KQHIIYIIDFGLAKEY 196
Cdd:cd14145   88 rGGPLNRV--LSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKVENgdlSNKILKITDFGLAREW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 idpethkhipYREHK-SLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRAT 275
Cdd:cd14145  166 ----------HRTTKmSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGI--DGLAVAY-GVAMNKLSL 232
                        250
                 ....*....|....
gi 919096895 276 PIEVLCenfPEELA 289
Cdd:cd14145  233 PIPSTC---PEPFA 243
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
47-219 3.91e-07

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: 51.41  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL-EYRFYKQLGQsEGVPQVY----YFGPCGKYNA- 117
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkirMENEKEGFPITAIrEIKLLQKLDH-PNVVRLKeivtSKGSAKYKGSi 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 -LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEY 196
Cdd:cd07840   80 yMVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLK-----LADFGLARPY 154
                        170       180
                 ....*....|....*....|....*....
gi 919096895 197 IDPE----THKHIP--YREHKSLTGTARY 219
Cdd:cd07840  155 TKENnadyTNRVITlwYRPPELLLGATRY 183
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
134-240 3.93e-07

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: 51.27  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 134 CDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHIIYIIDFGLAKEYidpeTHKHIPYrehkSL 213
Cdd:cd08220   94 KGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN----KKRTVVKIGDFGISKIL----SSKSKAY----TV 161
                         90       100
                 ....*....|....*....|....*..
gi 919096895 214 TGTARYMSINTHLGKEQSRRDDLEALG 240
Cdd:cd08220  162 VGTPCYISPELCEGKPYNQKSDIWALG 188
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
117-196 4.01e-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: 51.51  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSLEDLFDLC-DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd07838   82 TLVFEHVDQDLATYLDKCpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVK-----LADFGLARI 156

                 .
gi 919096895 196 Y 196
Cdd:cd07838  157 Y 157
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
47-269 4.25e-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: 51.01  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQLHLEYRFYKQLG-----QSEGVPQVY-YFGPCGKYNALVL 120
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD-RRRASPDFVQKFLPRELSilrrvNHPNIVQMFeCIEVANGRLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 EllgPSLEDLFDLCDRKFSLKTVLM--IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiIYIIDFGLAKEYID 198
Cdd:cd14164   81 E---AAATDLLQKIQEVHHIPKDLArdMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK----IKIADFGFARFVED 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 199 PETHKHipyrehkSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkeRYQKIG 269
Cdd:cd14164  154 YPELST-------TFCGSRAYTPPEVILGtPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRG 216
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
50-311 4.30e-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: 51.00  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ-----------LHLEYRFYKQLgQSEGVPQvyYFGPC--GKYN 116
Cdd:cd06628    5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmldaLQREIALLREL-QHENIVQ--YLGSSsdANHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELL-GPSLEDLFDLCDrKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKE 195
Cdd:cd06628   82 NIFLEYVpGGSVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG-----IKISDFGISKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 196 Y----IDPETHKHIPyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDT 271
Cdd:cd06628  156 LeansLSTKNNGARP-----SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQAIF-KIGEN 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 919096895 272 KRATPIevlcENFPEELATYLRYVRRLDFFETPDYDYLRK 311
Cdd:cd06628  228 ASPTIP----SNISSEARDFLEKTFEIDHNKRPTADELLK 263
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
118-249 4.42e-07

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: 51.53  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyi 197
Cdd:cd07872   81 LVFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELK-----LADFGLARA-- 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 919096895 198 dpethKHIPYREHKSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRG 249
Cdd:cd07872  154 -----KSVPTKTYSNEVVTLWYRPPDVLLGsSEYSTQIDMWGVGCIFFEMASG 201
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
106-195 4.54e-07

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: 51.08  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 106 VYYFGPCGKYNALVLEL--LGpSLEDLFDLCDRKF-SLKTVLM--IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAK 180
Cdd:cd14000   73 VYLLGIGIHPLMLVLELapLG-SLDHLLQQDSRSFaSLGRTLQqrIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPN 151
                         90
                 ....*....|....*
gi 919096895 181 KQHIIYIIDFGLAKE 195
Cdd:cd14000  152 SAIIIKIADYGISRQ 166
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
143-268 4.57e-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: 51.12  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 143 VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyidpethKHIPYREHKSLTGTARYMSI 222
Cdd:cd07870  100 VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELK-----LADFGLARA-------KSIPSQTYSSEVVTLWYRPP 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 919096895 223 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLkADTLkERYQKI 268
Cdd:cd07870  168 DVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPGV-SDVF-EQLEKI 212
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
118-261 4.80e-07

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: 51.17  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSleDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAke 195
Cdd:cd14194   85 LILELVAGG--ELFDFLAEKESLteEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPR-IKIIDFGLA-- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 196 yidpetHKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 261
Cdd:cd14194  160 ------HKIDFGNEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
106-242 5.15e-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: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 106 VYYFGPCGKYNAL--VLELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQ 182
Cdd:cd14065   51 LRFIGVCVKDNKLnfITEYVnGGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRN 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 183 HIiyIIDFGLAKEYIDPETHKhiPYR-EHKSLTGTARYMSINTHLGKEQSRRDDLEALGHM 242
Cdd:cd14065  131 AV--VADFGLAREMPDEKTKK--PDRkKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
47-195 5.53e-07

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: 50.67  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKQLgQSEGVpqVYYFGPCGKYNALVLELLGP 125
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARrELALLAEL-DHKSI--VRFHDAFEKRRVVIIVTELC 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 126 SLEDLFDLCDRKFSLKT-VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYIIDFGLAKE 195
Cdd:cd14108   81 HEELLERITKRPTVCESeVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQ---VRICDFGNAQE 148
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
39-288 5.85e-07

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: 51.54  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  39 GVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGK 114
Cdd:cd05621   46 ELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELL-GPSLEDL---FDLCDRKFSLKTVlmiaiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDF 190
Cdd:cd05621  126 YLYMVMEYMpGGDLVNLmsnYDVPEKWAKFYTA-----EVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLK-----LADF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 191 GLAKEyIDPETHKHIpyrehKSLTGTARYMSinTHLGKEQ------SRRDDLEALGHMFMYFLRGSLPWQglkADTLKER 264
Cdd:cd05621  196 GTCMK-MDETGMVHC-----DTAVGTPDYIS--PEVLKSQggdgyyGRECDWWSVGVFLFEMLVGDTPFY---ADSLVGT 264
                        250       260
                 ....*....|....*....|....
gi 919096895 265 YQKIGDTKRATpievlceNFPEEL 288
Cdd:cd05621  265 YSKIMDHKNSL-------NFPDDV 281
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
50-276 6.47e-07

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: 50.70  E-value: 6.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQLHL------EYRFYKQLGQSEGVPQVYYFGPcgkynalvlell 123
Cdd:cd14189    6 GRLLGKGGFARCYEMTDLATNKTYAVKVIP-HSRVAKPHQrekivnEIELHRDLHHKHVVKFSHHFED------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLCDRKfSL-------KTVLMIAI-----QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFG 191
Cdd:cd14189   73 AENIYIFLELCSRK-SLahiwkarHTLLEPEVryylkQIISGLKYLHLKGILHRDLKLGNFFINENMELK-----VGDFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 192 LAKEYIDPETHKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKadtLKERYQKIGDT 271
Cdd:cd14189  147 LAARLEPPEQRK-------KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLD---LKETYRCIKQV 216

                 ....*
gi 919096895 272 KRATP 276
Cdd:cd14189  217 KYTLP 221
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
146-253 6.59e-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: 50.42  E-value: 6.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKH-LIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEThkhipyrehKSLTGTARYMSINT 224
Cdd:cd06605  104 IAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVK-----LCDFGVSGQLVDSLA---------KTFVGTRSYMAPER 169
                         90       100
                 ....*....|....*....|....*....
gi 919096895 225 HLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06605  170 ISGGKYTVKSDIWSLGLSLVELATGRFPY 198
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-207 6.61e-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: 50.76  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMK--SRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLgpSLEDL 130
Cdd:cd14166   11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSplSRDSSLENEIAVLKRI-KHENIVTLEDIYESTTHYYLVMQLV--SGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 131 FD-LCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKE------------- 195
Cdd:cd14166   88 FDrILERGvYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLY--LTPDENSKIMITDFGLSKMeqngimstacgtp 165
                        170
                 ....*....|...
gi 919096895 196 -YIDPETHKHIPY 207
Cdd:cd14166  166 gYVAPEVLAQKPY 178
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
53-300 7.01e-07

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: 51.19  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKL--EPMKS--RAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNA-----LVLELL 123
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKlsRPFQSiiHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEfndvyLVTHLM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDlCdRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeYIDPETHK 203
Cdd:cd07877  105 GADLNNIVK-C-QKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELK-----ILDFGLAR-HTDDEMTG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 204 HIPYREHKSLTGTARYMSINTHLgkeqsrrdDLEALGHMFMYFLRGSLPWQGLK-ADTLKERYQKIGdtkraTPIEVLCE 282
Cdd:cd07877  177 YVATRWYRAPEIMLNWMHYNQTV--------DIWSVGCIMAELLTGRTLFPGTDhIDQLKLILRLVG-----TPGAELLK 243
                        250       260
                 ....*....|....*....|..
gi 919096895 283 NFPEELA-TY---LRYVRRLDF 300
Cdd:cd07877  244 KISSESArNYiqsLTQMPKMNF 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
52-219 7.04e-07

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: 50.75  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRAPQLHL-EYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLGPSL 127
Cdd:cd07835    6 KIGEGTYGVVYKARDKLTGEIVAlkkIRLETEDEGVPSTAIrEISLLKEL-NHPNIVRLLDVVHSENKLYLVFEFLDLDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCdRKFSL-----KTVLMiaiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDP--- 199
Cdd:cd07835   85 KKYMDSS-PLTGLdppliKSYLY---QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALK-----LADFGLARAFGVPvrt 155
                        170       180
                 ....*....|....*....|..
gi 919096895 200 ETHKHIP--YREHKSLTGTARY 219
Cdd:cd07835  156 YTHEVVTlwYRAPEILLGSKHY 177
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
49-299 7.57e-07

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: 50.43  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKnlYNNEhVAIKLEPMkSRAPQLHL-----EYRFYKQLgQSEGVpqVYYFGPCGKYN--ALVLE 121
Cdd:cd14063    4 IKEVIGKGRFGRVHRGR--WHGD-VAIKLLNI-DYLNEEQLeafkeEVAAYKNT-RHDNL--VLFMGACMDPPhlAIVTS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI--GRqsakkqhiIYIIDFGLAK--EY 196
Cdd:cd14063   77 LCkGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLenGR--------VVITDFGLFSlsGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 197 IDPETHKH---IPYrehksltGTARYMS--INTHLGKEQSRRDDLE--------ALGHMFMYFLRGSLPWQGLKADT--- 260
Cdd:cd14063  149 LQPGRREDtlvIPN-------GWLCYLApeIIRALSPDLDFEESLPftkasdvyAFGTVWYELLAGRWPFKEQPAESiiw 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 919096895 261 -----LKERYQKIGDTKRATPIEVLCENF-PEELATYLRYVRRLD 299
Cdd:cd14063  222 qvgcgKKQSLSQLDIGREVKDILMQCWAYdPEKRPTFSDLLRMLE 266
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
118-219 8.17e-07

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: 50.69  E-value: 8.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEY- 196
Cdd:cd07843   83 MVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG-----ILKICDFGLAREYg 157
                         90       100
                 ....*....|....*....|....*..
gi 919096895 197 --IDPETHKHIP--YREHKSLTGTARY 219
Cdd:cd07843  158 spLKPYTQLVVTlwYRAPELLLGAKEY 184
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
50-197 8.60e-07

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: 50.10  E-value: 8.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMK----SRApQLHLEYRFYKqLGQSEGVPQVYYFGPCGKYNALVLELlG 124
Cdd:cd14074    8 EETLGRGHFAVVKLARHVFTGEKVAVKvIDKTKlddvSKA-HLFQEVRCMK-LVQHPNVVRLYEVIDTQTKLYLILEL-G 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 125 PSlEDLFDLC---DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsAKKQHIIYIIDFGLAKEYI 197
Cdd:cd14074   85 DG-GDMYDYImkhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVF----FEKQGLVKLTDFGFSNKFQ 155
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
118-261 8.73e-07

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: 50.34  E-value: 8.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAke 195
Cdd:cd14196   85 LILELV--SGGELFDFLAQKESLseEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPH-IKLIDFGLA-- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 196 yidpetHKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 261
Cdd:cd14196  160 ------HEIEDGVEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
112-253 9.28e-07

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: 50.13  E-value: 9.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 112 CGKYNAlVLELLGPsledlfdlcdrkFSLKTVLMIAIQLVTRMEYVHSKH-LIYRDVKPENFLIgrqSAKKQhiIYIIDF 190
Cdd:cd06620   88 CGSLDK-ILKKKGP------------FPEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILV---NSKGQ--IKLCDF 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 191 GLAKEYIDPEThkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06620  150 GVSGELINSIA---------DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
46-258 9.61e-07

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: 50.04  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ-------LHLEYRFYKQLGQsEGVPQVYYF--GPCGKYN 116
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPEtskevnaLECEIQLLKNLLH-ERIVQYYGClrDPQERTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELL-GPSLED-------LFDLCDRKFSLktvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLigRQSAKKqhiIYII 188
Cdd:cd06652   82 SIFMEYMpGGSIKDqlksygaLTENVTRKYTR--------QILEGVHYLHSNMIVHRDIKGANIL--RDSVGN---VKLG 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 189 DFGLAKEYidpeTHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 258
Cdd:cd06652  149 DFGASKRL----QTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEA 214
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
118-268 9.64e-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: 50.41  E-value: 9.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLE-DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAke 195
Cdd:cd05630   77 LVLTLMnGGDLKfHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH-----IRISDLGLA-- 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 196 yidpethKHIPYREH-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKI 268
Cdd:cd05630  150 -------VHVPEGQTiKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERL 216
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
45-192 1.06e-06

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: 49.96  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  45 PNFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYR---FYKQLGQSEGVPQVY--------YFgpc 112
Cdd:cd14079    2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKiLNRQKIKSLDMEEKIRreiQILKLFRHPHIIRLYevietptdIF--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 gkynaLVLELLGPslEDLFDLCDRKFSLKTVLMIAI--QLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDF 190
Cdd:cd14079   79 -----MVMEYVSG--GELFDYIVQKGRLSEDEARRFfqQIISGVEYCHRHMVVHRDLKPENLLLDS-----NMNVKIADF 146

                 ..
gi 919096895 191 GL 192
Cdd:cd14079  147 GL 148
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
51-212 1.11e-06

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: 50.26  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSR--APQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPS 126
Cdd:cd07856   16 QPVGMGAFGLVCSARDQLTGQNVAVKkiMKPFSTPvlAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeYIDPETHKHIP 206
Cdd:cd07856   96 LHRL--LTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLK-----ICDFGLAR-IQDPQMTGYVS 167

                 ....*.
gi 919096895 207 YREHKS 212
Cdd:cd07856  168 TRYYRA 173
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
51-254 1.17e-06

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: 49.60  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQlgqsegvPQVYYFGPC---GKYNALVLELl 123
Cdd:cd14665    6 KDIGSGNFGVARLMRDKQTKELVAVKYiergEKIDENVQREIINHRSLRH-------PNIVRFKEViltPTHLAIVMEY- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 gPSLEDLFD-LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYIIDFGLAKEyidpet 201
Cdd:cd14665   78 -AAGGELFErICNAgRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPR---LKICDFGYSKS------ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919096895 202 hkHIPYREHKSLTGTARYMSINTHLGKE-QSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14665  148 --SVLHSQPKSTVGTPAYIAPEVLLKKEyDGKIADVWSCGVTLYVMLVGAYPFE 199
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
118-213 1.19e-06

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: 49.65  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLEL--LGPSLEDLFDLCDRkFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQhiIYIIDFGLAKE 195
Cdd:cd05040   74 MVTELapLGSLLDRLRKDQGH-FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILL---ASKDK--VKIGDFGLMRA 147
                         90
                 ....*....|....*...
gi 919096895 196 YidPETHKHIPYREHKSL 213
Cdd:cd05040  148 L--PQNEDHYVMQEHRKV 163
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
47-195 1.21e-06

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 49.99  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVY--YF--GPCGKYNAL--V 119
Cdd:cd06608    8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKiMDIIEDEEEEIKLEINILRKFSNHPNIATFYgaFIkkDPPGGDDQLwlV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELL-GPSLEDL---FDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd06608   88 MEYCgGGSVTDLvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVK-----LVDFGVSAQ 162
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
50-195 1.21e-06

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: 49.62  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGkNLYNNEHVAIKlePMKSRAPQlHLEYRFYKQ---LGQSEGVPQVYYFGPCGKYNA--LVLELLg 124
Cdd:cd05085    1 GELLGKGNFGEVYKG-TLKDKTPVAVK--TCKEDLPQ-ELKIKFLSEariLKQYDHPNIVKLIGVCTQRQPiyIVMELV- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 125 PSLEDLFDLCDRKFSLKT--VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd05085   76 PGGDFLSFLRKKKDELKTkqLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALK-----ISDFGMSRQ 143
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
46-261 1.23e-06

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: 50.31  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL--------------EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFgp 111
Cdd:cd05619    6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKAlkkdvvlmdddvecTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFF-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 112 cgkynalVLELL-GPSLEDLFDLCdRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDF 190
Cdd:cd05619   84 -------VMEYLnGGDLMFHIQSC-HKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-----IKIADF 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 191 GLAKEYI--DPEThkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05619  151 GMCKENMlgDAKT---------STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEEL 214
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
46-219 1.39e-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: 49.81  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRAPQLHL-EYRFYKQLGQSEGVpQVYYFGPCGKYNALVLE 121
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKARNKLTGEVVAlkkIRLDTETEGVPSTAIrEISLLKELNHPNIV-KLLDVIHTENKLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLGPSLEDLFDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDP- 199
Cdd:cd07860   80 FLHQDLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA-----IKLADFGLARAFGVPv 154
                        170       180
                 ....*....|....*....|....
gi 919096895 200 ETHKH----IPYREHKSLTGTARY 219
Cdd:cd07860  155 RTYTHevvtLWYRAPEILLGCKYY 178
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
132-274 1.41e-06

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.98  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 132 DLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKE-YIDPETHKhipyreh 210
Cdd:cd05103  170 DLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLS-----ENNVVKICDFGLARDiYKDPDYVR------- 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 211 kslTGTAR----YMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRA 274
Cdd:cd05103  238 ---KGDARlplkWMAPETIFDRVYTIQSDVWSFGvLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRA 303
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
53-221 1.46e-06

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: 49.71  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMK-SRAPQ-LHLEYRFYKQLgQSEGVpqVYYFGPC--GKYNALVLELL-GPSL 127
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPERdSREVQpLHEEIALHSRL-SHKNI--VQYLGSVseDGFFKIFMEQVpGGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLfdLCDRKFSLK----TVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhIIYIIDFGLAKEY--IDPET 201
Cdd:cd06624   93 SAL--LRSKWGPLKdnenTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSG----VVKISDFGTSKRLagINPCT 166
                        170       180
                 ....*....|....*....|
gi 919096895 202 hkhipyrehKSLTGTARYMS 221
Cdd:cd06624  167 ---------ETFTGTLQYMA 177
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
47-253 1.50e-06

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: 49.56  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGK-YNAL------- 118
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPLERvYQEIailkkld 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 ------VLELLGPSLED----LFDL----------CDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQS 178
Cdd:cd14200   82 hvnivkLIEVLDDPAEDnlymVFDLlrkgpvmevpSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 179 AKKqhiiyIIDFGLAKEYIDPEThkhipyrEHKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd14200  162 HVK-----IADFGVSNQFEGNDA-------LLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPF 227
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
118-221 1.50e-06

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: 49.66  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgPSLEdLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKE 195
Cdd:cd14093   86 LVFELC-RKGE-LFDYLTEVvtLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL-----DDNLNVKISDFGFATR 158
                         90       100
                 ....*....|....*....|....*.
gi 919096895 196 yIDPEthkhipyREHKSLTGTARYMS 221
Cdd:cd14093  159 -LDEG-------EKLRELCGTPGYLA 176
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
46-200 1.60e-06

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: 49.88  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPM--KSRAPQLHLEyRFYKQLGQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd05610    5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVvkkADMinKNMVHQVQAE-RDALALSKSPFIVHLYYSLQSANNVYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 E-LLG---PSLEDLFDLCDRKFSLKTVLMIAIQLvtrmEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEY 196
Cdd:cd05610   84 EyLIGgdvKSLLHIYGYFDEEMAVKYISEVALAL----DYLHRHGIIHRDLKPDNMLISNEG----H-IKLTDFGLSKVT 154

                 ....
gi 919096895 197 IDPE 200
Cdd:cd05610  155 LNRE 158
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
137-261 1.81e-06

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: 49.69  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYIdpethkhipYREHKSLT-- 214
Cdd:cd05592   92 RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREG----H-IKIADFGMCKENI---------YGENKASTfc 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 919096895 215 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05592  158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDEL 204
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
138-253 1.97e-06

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: 49.53  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 138 FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHIIyIIDFGLAKEYIDPETHKHIpyrehkSLTGTA 217
Cdd:cd05614  102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEG----HVV-LTDFGLSKEFLTEEKERTY------SFCGTI 170
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 919096895 218 RYMSINTHLGKE-QSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05614  171 EYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPF 207
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
53-194 2.09e-06

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: 48.79  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGknLYNNEHVAIKLEpmksrapQLHLEYRFYKQ----LGQSEGVPQVYYFGPCGKYNALVLELLGP-SL 127
Cdd:cd14068    2 LGDGGFGSVYRA--VYRGEDVAVKIF-------NKHTSFRLLRQelvvLSHLHHPSLVALLAAGTAPRMLVMELAPKgSL 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHIIYIIDFGLAK 194
Cdd:cd14068   73 DALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIAKIADYGIAQ 139
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
46-258 2.27e-06

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: 48.87  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ-------LHLEYRFYKQLGQSEgvpQVYYFG----PCGK 114
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQEtskevnaLECEIQLLKNLRHDR---IVQYYGclrdPEEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELL-GPSLED-------LFDLCDRKFSLktvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLigRQSAKKqhiIY 186
Cdd:cd06653   80 KLSIFVEYMpGGSVKDqlkaygaLTENVTRRYTR--------QILQGVSYLHSNMIVHRDIKGANIL--RDSAGN---VK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 187 IIDFGLAKEYidpethkHIPYREH---KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 258
Cdd:cd06653  147 LGDFGASKRI-------QTICMSGtgiKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEA 214
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
46-200 2.43e-06

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 48.73  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGknLYNN-EHVAIKLEPMKSRAPQLHL-EYRFYKQLGQSEGVpqvyyfgpcgKYNALVLE-- 121
Cdd:cd05067    8 TLKLVERLGAGQFGEVWMG--YYNGhTKVAIKSLKQGSMSPDAFLaEANLMKQLQHQRLV----------RLYAVVTQep 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 -------LLGPSLEDLFDLCD-RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd05067   76 iyiiteyMENGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCK-----IADFGLA 150

                 ....*..
gi 919096895 194 KEYIDPE 200
Cdd:cd05067  151 RLIEDNE 157
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
47-200 2.60e-06

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: 49.23  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLepMKSRAPQLHLEYRFYKQ------LGQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKV--LKKSETLAQEEVSFFEEerdimaKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL--GpsleDLFDLCDR----------KFSLKTvLMIAIQLVTRMEYVHskhliyRDVKPENFLIGRqsakKQHiIYII 188
Cdd:cd05601   81 EYHpgG----DLLSLLSRyddifeesmaRFYLAE-LVLAIHSLHSMGYVH------RDIKPENILIDR----TGH-IKLA 144
                        170       180
                 ....*....|....*....|....*....
gi 919096895 189 DFGLA-----------------KEYIDPE 200
Cdd:cd05601  145 DFGSAaklssdktvtskmpvgtPDYIAPE 173
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
47-316 2.67e-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: 48.87  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKnlYNNEHVAIKL------EPMKSRAPQLHLEYRFYKQLGQsegvPQVYYF-GPCGKYNALV 119
Cdd:cd14147    5 LRLEEVIGIGGFGKVYRGS--WRGELVAVKAarqdpdEDISVTAESVRQEARLFAMLAH----PNIIALkAVCLEEPNLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLGPSLEDLFD-LCDRKFSLKTVLMIAIQLVTRMEYVHSKHL---IYRDVKPENFLI---GRQSAKKQHIIYIIDFGL 192
Cdd:cd14147   79 LVMEYAAGGPLSRaLAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLlqpIENDDMEHKTLKITDFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 193 AKEYidpetHKhipyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTK 272
Cdd:cd14147  159 AREW-----HK----TTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGI--DCLAVAY-GVAVNK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 919096895 273 RATPIEVLCenfPEELATYLRYVRRLDFFETPDYDYLRKLFTDL 316
Cdd:cd14147  227 LTLPIPSTC---PEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
52-240 2.84e-06

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: 48.88  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIKlePMKSRAPQLH-------LEYRFYKQLGQSEGVPqvyYFGPCGKYNA--LVLEL 122
Cdd:cd06633   28 EIGHGSFGAVYFATNSHTNEVVAIK--KMSYSGKQTNekwqdiiKEVKFLQQLKHPNTIE---YKGCYLKDHTawLVMEY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LGPSLEDLFDLcdRKFSLKTVLMIAIQ--LVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAkEYIDPE 200
Cdd:cd06633  103 CLGSASDLLEV--HKKPLQEVEIAAIThgALQGLAYLHSHNMIHRDIKAGNILLTEPGQVK-----LADFGSA-SIASPA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 919096895 201 ThkhipyrehkSLTGTARYMSINTHLGKEQSRRD---DLEALG 240
Cdd:cd06633  175 N----------SFVGTPYWMAPEVILAMDEGQYDgkvDIWSLG 207
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
102-191 3.12e-06

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: 46.67  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 102 GVPQVYYFGPCGKYNALVLELL-GPSLEDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaK 180
Cdd:cd13968   53 NIPKVLVTEDVDGPNILLMELVkGGTLIAY--TQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL-----S 125
                         90
                 ....*....|.
gi 919096895 181 KQHIIYIIDFG 191
Cdd:cd13968  126 EDGNVKLIDFG 136
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
46-193 3.27e-06

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: 48.27  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKS------------RAPQLHleyrfykQLGQSEGVPQVYYFGPCG 113
Cdd:cd14070    3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKakkdsyvtknlrREGRIQ-------QMIRHPNITQLLDILETE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 KYNALVLEL-LGPSLEDlfDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFG 191
Cdd:cd14070   76 NSYYLVMELcPGGNLMH--RIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN-----IKLIDFG 148

                 ..
gi 919096895 192 LA 193
Cdd:cd14070  149 LS 150
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
90-202 3.37e-06

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 46.88  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  90 EYRFYKQLgQSEG--VPQVYYFGPCGKYnaLVLELL-GPSLEDLFDlcdrKFSLKTVLMIAI-QLVTRMeyvHSKHLIYR 165
Cdd:COG3642    6 EARLLREL-REAGvpVPKVLDVDPDDAD--LVMEYIeGETLADLLE----EGELPPELLRELgRLLARL---HRAGIVHG 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 919096895 166 DVKPENFLIGRQSakkqhiIYIIDFGLAKEYIDPETH 202
Cdd:COG3642   76 DLTTSNILVDDGG------VYLIDFGLARYSDPLEDK 106
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
118-209 3.43e-06

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: 48.27  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLEDLFDLCDRK---FSLKTVLMIAIQLVTRMEYVH-SKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGL 192
Cdd:cd08528   86 IVMELIeGAPLGEHFSSLKEKnehFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK-----VTITDFGL 160
                         90       100       110
                 ....*....|....*....|....*....|...
gi 919096895 193 AKE----------------YIDPETHKHIPYRE 209
Cdd:cd08528  161 AKQkgpesskmtsvvgtilYSCPEIVQNEPYGE 193
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
135-197 3.51e-06

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: 48.89  E-value: 3.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYI 197
Cdd:cd05571   89 ERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDG----H-IKITDFGLCKEEI 146
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
50-301 3.65e-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: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQLHL------EYRFYKQLGQSEGVPQVYYFGpcGKYNALVLell 123
Cdd:cd14188    6 GKVLGKGGFAKCYEMTDLTTNKVYAAKIIP-HSRVSKPHQrekidkEIELHRILHHKHVVQFYHYFE--DKENIYIL--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 gpsledlFDLCDRK---FSLKT--------VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGL 192
Cdd:cd14188   80 -------LEYCSRRsmaHILKArkvltepeVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELK-----VGDFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 193 AKEyIDPETHKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTK 272
Cdd:cd14188  148 AAR-LEPLEHR------RRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE---TTNLKETYRCIREAR 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 919096895 273 RATP----------IEVLCENFPEElATYLRYVRRLDFF 301
Cdd:cd14188  218 YSLPssllapakhlIASMLSKNPED-RPSLDEIIRHDFF 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
118-261 3.72e-06

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: 48.46  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAke 195
Cdd:cd14195   85 LILELV--SGGELFDFLAEKESLteEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPR-IKLIDFGIA-- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 196 yidpetHKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 261
Cdd:cd14195  160 ------HKIEAGNEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGeTKQETL 220
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
47-193 3.95e-06

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 48.40  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQLgQSEGVPQvyYFGPCGKYNAL--VLE 121
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKvidLEEAEDEIEDIQQEIQFLSQC-DSPYITK--YYGSFLKGSKLwiIME 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 122 LL-GPSLEDLFDLCdrKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd06609   80 YCgGGSVLDLLKPG--PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVK-----LADFGVS 145
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
118-240 4.00e-06

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: 48.15  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLeDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKe 195
Cdd:cd14004   85 LVMEKHGSGM-DLFDFIERKPNMdeKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIK-----LIDFGSAA- 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 196 YIDPEthkhiPYrehKSLTGTARYMSI-----NTHLGKEQsrrdDLEALG 240
Cdd:cd14004  158 YIKSG-----PF---DTFVGTIDYAAPevlrgNPYGGKEQ----DIWALG 195
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
51-206 4.61e-06

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: 47.82  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHlEYRFYKQLGQsegvPQ-VYYFGPCGKYNAL--VLELL 123
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKTcretLPPDLKRKFLQ-EARILKQYDH----PNiVKLIGVCVQKQPImiVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDFGLAKE-----YI 197
Cdd:cd05041   76 pGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGE-----NNVLKISDFGMSREeedgeYT 150

                 ....*....
gi 919096895 198 DPETHKHIP 206
Cdd:cd05041  151 VSDGLKQIP 159
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
118-194 4.74e-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: 48.45  E-value: 4.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 118 LVLELLgpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAK 194
Cdd:cd14092   76 LVMELL--RGGELLERIRKKkrFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLF--TDEDDDAEIKIVDFGFAR 150
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
42-287 4.99e-06

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 48.46  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  42 MVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNA 117
Cdd:cd05622   70 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLEDLFDLCDrkFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGL---- 192
Cdd:cd05622  150 MVMEYMpGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK-----LADFGTcmkm 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 193 -------------AKEYIDPEThkhipyreHKSLTGTARYmsinthlgkeqSRRDDLEALGHMFMYFLRGSLPWQglkAD 259
Cdd:cd05622  223 nkegmvrcdtavgTPDYISPEV--------LKSQGGDGYY-----------GRECDWWSVGVFLYEMLVGDTPFY---AD 280
                        250       260
                 ....*....|....*....|....*...
gi 919096895 260 TLKERYQKIGDTKRATpievlceNFPEE 287
Cdd:cd05622  281 SLVGTYSKIMNHKNSL-------TFPDD 301
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-212 5.17e-06

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: 48.16  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMKSR-APQLHLEYRFYKQLGQS--EGVPQV------YYFGpcgKYNALVLELL 123
Cdd:cd14225   51 IGKGSFGQVVKALDHKTNEHVAIKIIRNKKRfHHQALVEVKILDALRRKdrDNSHNVihmkeyFYFR---NHLCITFELL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLCD-RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHIIYIIDFGlAKEYIDPETH 202
Cdd:cd14225  128 GMNLYELIKKNNfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILL---RQRGQSSIKVIDFG-SSCYEHQRVY 203
                        170
                 ....*....|
gi 919096895 203 KHIPYREHKS 212
Cdd:cd14225  204 TYIQSRFYRS 213
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
52-194 5.54e-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: 47.75  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLH----LEYRFYKQLGQSEGVPQVYYFGPCGKYNaLVLELLGPSL 127
Cdd:cd07847    8 KIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKkialREIRMLKQLKHPNLVNLIEVFRRKRKLH-LVFEYCDHTV 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK 194
Cdd:cd07847   87 LNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILI-----TKQGQIKLCDFGFAR 148
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
46-315 5.63e-06

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: 47.76  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGkNLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKQLGQSEGVPQVYYFGPCGKYnaLVLELLG 124
Cdd:cd05069   13 SLRLDVKLGQGCFGEVWMG-TWNGTTKVAIKTLKPGTMMPEAFLqEAQIMKKLRHDKLVPLYAVVSEEPIY--IVTEFMG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 P-SLEDLFDLCDRKF-SLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEth 202
Cdd:cd05069   90 KgSLLDFLKEGDGKYlKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCK-----IADFGLARLIEDNE-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 khipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLKADTLKERYqkigDTKRATPIEVLC 281
Cdd:cd05069  163 ----YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMVNREVLEQV----ERGYRMPCPQGC 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 919096895 282 enfPEELATYLRYVRRLDFFETPDYDYLRKLFTD 315
Cdd:cd05069  235 ---PESLHELMKLCWKKDPDERPTFEYIQSFLED 265
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
118-194 5.66e-06

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: 47.76  E-value: 5.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd07844   75 LVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELK-----LADFGLAR 146
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
47-272 6.34e-06

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 47.70  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEyrFYKQLGQSEGVPQVYYFGPCGKYNALVLELL-GP 125
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIE--ILMRYGQHPNIITLKDVYDDGRYVYLVTELMkGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIIDFGLAKEYIDPETHKHI 205
Cdd:cd14177   84 ELLDRI-LRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADS-IRICDFGFAKQLRGENGLLLT 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 206 PyrehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 272
Cdd:cd14177  162 P-------CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGK 221
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
46-194 6.45e-06

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: 47.62  E-value: 6.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLePMKSRApqlhleyRFYKQLGQSEGVPQ-VYYFGPCGKYN-------- 116
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKF-VPKSRV-------TEWAMINGPVPVPLeIALLLKASKPGvpgvirll 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ---------ALVLELLGPSlEDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHII 185
Cdd:cd14005   73 dwyerpdgfLLIMERPEPC-QDLFDFITERGALseNLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLIN----LRTGEV 147

                 ....*....
gi 919096895 186 YIIDFGLAK 194
Cdd:cd14005  148 KLIDFGCGA 156
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
144-247 6.52e-06

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: 47.49  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 144 LMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQhiIYIIDFGLAKEYIDPethkhIPYREHKsltGTARYMSIN 223
Cdd:cd14047  120 LEIFEQITKGVEYIHSKKLIHRDLKPSNIFL---VDTGK--VKIGDFGLVTSLKND-----GKRTKSK---GTLSYMSPE 186
                         90       100
                 ....*....|....*....|....
gi 919096895 224 THLGKEQSRRDDLEALGHMFMYFL 247
Cdd:cd14047  187 QISSQDYGKEVDIYALGLILFELL 210
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
53-196 6.85e-06

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: 47.26  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRApQLHLEYRFYKQLGQSEGVpQVYYFGPCGKYNALVLELLGPSleD 129
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAakiIKVKGAKERE-EVKNEINIMNQLNHVNLI-QLYDAFESKTNLTLIMEYVDGG--E 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFD-LCDRKFSLKT--VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqHIIYIIDFGLAKEY 196
Cdd:cd14192   88 LFDrITDESYQLTEldAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTG---NQIKIIDFGLARRY 154
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
51-194 6.86e-06

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: 47.62  E-value: 6.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRL------GKNlyNNEHVAIK-LEPMK--SRAPQLHLEYRFYKQLgQSEGVpqVYYFGPC----GKYNA 117
Cdd:cd05079   10 RDLGEGHFGKVELcrydpeGDN--TGEQVAVKsLKPESggNHIADLKKEIEILRNL-YHENI--VKYKGICtedgGNGIK 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 118 LVLELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK 194
Cdd:cd05079   85 LIMEFLpSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-----ESEHQVKIGDFGLTK 157
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
53-224 7.38e-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: 47.44  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK-----LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELL---- 123
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqeLSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPNDLPLLamey 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 --GPSLEDLFDLCDRKFSLKT--VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhIIY-IIDFGLAKE--- 195
Cdd:cd13989   81 csGGDLRKVLNQPENCCGLKEseVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGR---VIYkLIDLGYAKEldq 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 919096895 196 ------------YIDPETHKHIPYrehkslTGTARYMSINT 224
Cdd:cd13989  158 gslctsfvgtlqYLAPELFESKKY------TCTVDYWSFGT 192
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
124-193 7.43e-06

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: 47.39  E-value: 7.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 124 GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPEN-FLIGRQSAKkqhiiyIIDFGLA 193
Cdd:cd14062   72 GSSLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNiFLHEDLTVK------IGDFGLA 136
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-207 7.51e-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: 47.37  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEYRFYKQLGQSEGV--------PQVYYfgpcgkynaLVLE 121
Cdd:cd14083   11 LGTGAFSEVVLAEDKATGKLVAIKCidkKALKGKEDSLENEIAVLRKIKHPNIVqlldiyesKSHLY---------LVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LLgpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAK----- 194
Cdd:cd14083   82 LV--TGGELFDRIVEKgsYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLY--YSPDEDSKIMISDFGLSKmedsg 157
                        170       180
                 ....*....|....*....|..
gi 919096895 195 ---------EYIDPETHKHIPY 207
Cdd:cd14083  158 vmstacgtpGYVAPEVLAQKPY 179
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
46-191 7.77e-06

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 47.76  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd05596   27 DFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLlskfEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMD 106
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 122 LL-GPSLEDLFDLCDrkFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFG 191
Cdd:cd05596  107 YMpGGDLVNLMSNYD--VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLK-----LADFG 170
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
46-264 7.87e-06

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: 47.43  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNN-EHVAIKLEP----------MKSRApQLHLEYRFYKQLGQSEgVPQVYYFGPCGK 114
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVPLRNTgKPVAIKVVRkadlssdnlkGSSRA-NILKEVQIMKRLSHPN-IVKLLDFQESDE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELLGPSleDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFL-----IGRQSAKKQH---- 183
Cdd:cd14096   80 YYYIVLELADGG--EIFHQIVRltYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipFIPSIVKLRKaddd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 184 -------------------IIYIIDFGLAKEYIDPEThkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFM 244
Cdd:cd14096  158 etkvdegefipgvggggigIVKLADFGLSKQVWDSNT---------KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLY 228
                        250       260
                 ....*....|....*....|
gi 919096895 245 YFLRGSLPWQGLKADTLKER 264
Cdd:cd14096  229 TLLCGFPPFYDESIETLTEK 248
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
149-279 7.87e-06

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: 47.28  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHIIYIIDFGLAKeYIDPETHKHipyrehkSLTGTARYMSINTHLGK 228
Cdd:cd14121  103 QLASALQFLREHNISHMDLKPQNLLL---SSRYNPVLKLADFGFAQ-HLKPNDEAH-------SLRGSPLYMAPEMILKK 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 229 EQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKIgdtKRATPIEV 279
Cdd:cd14121  172 KYDARVDLWSVG-VILYeCLFGRAPF---ASRSFEELEEKI---RSSKPIEI 216
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
135-263 7.89e-06

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: 47.77  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYI-DPEThkhipyreHKSL 213
Cdd:cd05593  109 ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-----IKITDFGLCKEGItDAAT--------MKTF 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 214 TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 263
Cdd:cd05593  176 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 225
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
51-219 8.44e-06

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: 47.41  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVA---IKLEPMKSRAPQLHL-EYRFYKQLGQSEGV---------PQVYyfgpcgkyna 117
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAmkkIRLESEEEGVPSTAIrEISLLKELQHPNIVcledvlmqeNRLY---------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLC--DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKE 195
Cdd:cd07861   76 LVFEFLSMDLKKYLDSLpkGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLI-----DNKGVIKLADFGLARA 150
                        170       180
                 ....*....|....*....|....*....
gi 919096895 196 YIDP---ETHKHIP--YREHKSLTGTARY 219
Cdd:cd07861  151 FGIPvrvYTHEVVTlwYRAPEVLLGSPRY 179
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
47-191 8.57e-06

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: 47.15  E-value: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMK-----SRAPQLH---LEYRFYKQLGQSEGVPQV-----YYFGPCG 113
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNrvqqwSKLPGVNpvpNEVALLQSVGGGPGHRGVirlldWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 KYnaLVLELLGPSlEDLFDLCDRKFSLKTVL--MIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiIYIIDFG 191
Cdd:cd14101   82 FL--LVLERPQHC-QDLFDYITERGALDESLarRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGD----IKLIDFG 154
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
53-293 8.82e-06

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: 47.34  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKnlYNNEHVAIKL------EPMKSRAPQLHLEYRFYKQLGQS-----EGV----PQ---VYYFGPCGK 114
Cdd:cd14146    2 IGVGGFGKVYRAT--WKGQEVAVKAarqdpdEDIKATAESVRQEAKLFSMLRHPniiklEGVcleePNlclVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YN-ALVLELLGPSLEDlfdlcDRKFSLKTVLMIAIQLVTRMEYVHSKH---LIYRDVKPENFL---------IGRQSAKk 181
Cdd:cd14146   80 LNrALAAANAAPGPRR-----ARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILllekiehddICNKTLK- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 182 qhiiyIIDFGLAKEYidpethkhipYREHK-SLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDT 260
Cdd:cd14146  154 -----ITDFGLAREW----------HRTTKmSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI--DG 216
                        250       260       270
                 ....*....|....*....|....*....|...
gi 919096895 261 LKERYqKIGDTKRATPIEVLCenfPEELATYLR 293
Cdd:cd14146  217 LAVAY-GVAVNKLTLPIPSTC---PEPFAKLMK 245
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
129-196 9.82e-06

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: 46.83  E-value: 9.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 129 DLFD-LCDRKFSLK---TVLMIAiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYIIDFGLAKEY 196
Cdd:cd14193   87 ELFDrIIDENYNLTeldTILFIK-QICEGIQYMHQMYILHLDLKPENILCVSREANQ---VKIIDFGLARRY 154
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
51-194 1.03e-05

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: 47.20  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSR--APQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALV-LELLGP 125
Cdd:cd07879   21 KQVGSGAYGSVCSAIDKRTGEKVAIKklSRPFQSEifAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQdFYLVMP 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLE-DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd07879  101 YMQtDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELK-----ILDFGLAR 165
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
130-293 1.10e-05

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: 46.72  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRKFSLKTVLMI--AIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKEYIDPEThkhipy 207
Cdd:cd14059   68 LYEVLRAGREITPSLLVdwSKQIASGMNYLHLHKIIHRDLKSPNVLVT-----YNDVLKISDFGTSKELSEKST------ 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 208 reHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkerYQKIGDTKRATPIEVLCenfPEE 287
Cdd:cd14059  137 --KMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAI---IWGVGSNSLQLPVPSTC---PDG 208

                 ....*.
gi 919096895 288 LATYLR 293
Cdd:cd14059  209 FKLLMK 214
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
47-252 1.16e-05

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: 46.99  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNAL--VLELLG 124
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLwiIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 P-SLEDLFDlcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETHK 203
Cdd:cd06641   86 GgSALDLLE--PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVK-----LADFGVAGQLTDTQIKR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 919096895 204 HipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06641  159 N-------*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
51-316 1.19e-05

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 46.96  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGknLYNNE-HVAIK-LEPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELL--GPS 126
Cdd:cd05072   13 KKLGAGQFGEVWMG--YYNNStKVAVKtLKPGTMSVQAFLEEANLMKTL-QHDKLVRLYAVVTKEEPIYIITEYMakGSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK-----EYIDPET 201
Cdd:cd05072   90 LDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCK-----IADFGLARviednEYTAREG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 202 HKH-IPYREHKSLTgtarYMSINThlgkeqsrRDDLEALGHMFMYFLR-GSLPWQGLKADTLKERYQKIGDTKRAtpiev 279
Cdd:cd05072  165 AKFpIKWTAPEAIN----FGSFTI--------KSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGYRMPRM----- 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 919096895 280 lcENFPEELATYLRYVRRLDFFETPDYDYLRKLFTDL 316
Cdd:cd05072  228 --ENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDF 262
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
130-293 1.27e-05

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: 46.75  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYidPETHKhipyre 209
Cdd:cd05577   84 IYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH-----VRISDLGLAVEF--KGGKK------ 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 210 HKSLTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQGLKADTLKEryqkigDTKRAT---PIEvLCENFP 285
Cdd:cd05577  151 IKGRVGTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKE------ELKRRTlemAVE-YPDSFS 223

                 ....*...
gi 919096895 286 EELATYLR 293
Cdd:cd05577  224 PEARSLCE 231
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
53-194 1.31e-05

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: 46.90  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK--LEPMKS--RAPQLHLEYRFYKQLGQ---------------SEGVPQVYyfgpcg 113
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTGRKVAIKklSRPFQSaiHAKRTYRELRLLKHMKHenviglldvftpassLEDFQDVY------ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 kynaLVLELLGPSLEDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd07851   97 ----LVTHLMGADLNNI--VKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELK-----ILDFGLA 165

                 .
gi 919096895 194 K 194
Cdd:cd07851  166 R 166
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
51-256 1.37e-05

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: 46.59  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNAL--VLELLGP-SL 127
Cdd:cd06642   10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLwiIMEYLGGgSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETHKHipy 207
Cdd:cd06642   90 LDL--LKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVK-----LADFGVAGQLTDTQIKRN--- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 919096895 208 rehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGL 256
Cdd:cd06642  160 ----TFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL 204
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
118-265 1.37e-05

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: 46.64  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLEDLF-DLCDRKFSLKTVLMIAIQlvtRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd06654   94 VVMEYLaGGSLTDVVtETCMDEGQIAAVCRECLQ---ALEFLHSNQVIHRDIKSDNILLGMDGSVK-----LTDFGFCAQ 165
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 196 yIDPETHKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 265
Cdd:cd06654  166 -ITPEQSK------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRALY 226
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
47-228 1.49e-05

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: 46.15  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHL----EYRFYKQLGQSEGVPQVYYFGPCGKYNALVLEL 122
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKrkleEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LGPSLEDLFDLCDrKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyIDPETH 202
Cdd:cd14050   83 CDTSLQQYCEETH-SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCK-----LGDFGLVVE-LDKEDI 155
                        170       180
                 ....*....|....*....|....*....
gi 919096895 203 KHIpyrehksLTGTARYMS---INTHLGK 228
Cdd:cd14050  156 HDA-------QEGDPRYMApelLQGSFTK 177
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
141-252 1.50e-05

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: 46.65  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 141 KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEThkhipyrehKSLTGTARYM 220
Cdd:cd06621  105 KVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVK-----LCDFGVSGELVNSLA---------GTFTGTSYYM 170
                         90       100       110
                 ....*....|....*....|....*....|..
gi 919096895 221 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06621  171 APERIQGGPYSITSDVWSLGLTLLEVAQNRFP 202
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
53-221 1.52e-05

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: 46.28  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRlgKNLYNNEHVAIKLEPMKSRAPQLHLEYRfykQLGQSEGVPQVYYFGPCGKYNA--LVLELL-GPSLED 129
Cdd:cd14058    1 VGRGSFGVVC--KARWRNQIVAVKIIESESEKKAFEVEVR---QLSRVDHPNIIKLYGACSNQKPvcLVMEYAeGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRK--FSLKTVLMIAIQLVTRMEYVHS---KHLIYRDVKPENFLIGRQSAkkqhIIYIIDFGLAkeyIDPETHKh 204
Cdd:cd14058   76 VLHGKEPKpiYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGT----VLKICDFGTA---CDISTHM- 147
                        170
                 ....*....|....*..
gi 919096895 205 ipyrehKSLTGTARYMS 221
Cdd:cd14058  148 ------TNNKGSAAWMA 158
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
47-195 1.65e-05

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: 46.87  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSR--APQLHLEYRFYKQLGQSEGVPQVYYFGP---CGKYNA-- 117
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKklYRPFQSElfAKRAYRELRLLKHMKHENVIGLLDVFTPdlsLDRFHDfy 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 118 LVLELLGPSLEDLFDLcdRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd07880   97 LVMPFMGTDLGKLMKH--EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELK-----ILDFGLARQ 167
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
47-193 1.65e-05

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: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL-EPMKSRAPQlHL---EYRFYKQLGQSEGVPQVYYFG-PCGKYnaLVLE 121
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIiDKAKCCGKE-HLienEVSILRRVKHPNIIMLIEEMDtPAELY--LVME 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 122 LLGPSleDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrQSAKKQHIIYIIDFGLA 193
Cdd:cd14184   80 LVKGG--DLFDaiTSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVC-EYPDGTKSLKLGDFGLA 150
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
128-298 1.66e-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. 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: 46.33  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKE-YIDPETHKhip 206
Cdd:cd05054  125 EDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLS-----ENNVVKICDFGLARDiYKDPDYVR--- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 207 yrehkslTGTAR----YMSINTHLGKEQSRRDDLEALGhMFMY--FLRGSLPWQGLKADtlKERYQKIGDTKR------A 274
Cdd:cd05054  197 -------KGDARlplkWMAPESIFDKVYTTQSDVWSFG-VLLWeiFSLGASPYPGVQMD--EEFCRRLKEGTRmrapeyT 266
                        170       180
                 ....*....|....*....|....*....
gi 919096895 275 TP----IEVLC-ENFPEELATYLRYVRRL 298
Cdd:cd05054  267 TPeiyqIMLDCwHGEPKERPTFSELVEKL 295
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
113-194 1.70e-05

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: 46.15  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 GKYN-ALVLELLgpSLEDLFD-LCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiIYII 188
Cdd:cd14191   70 EKANiVMVLEMV--SGGELFErIIDEDFELteRECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK---IKLI 144

                 ....*.
gi 919096895 189 DFGLAK 194
Cdd:cd14191  145 DFGLAR 150
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
149-221 1.74e-05

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: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYiDPETHKHIP-------YREHKSLTGTARYMS 221
Cdd:cd07853  111 QILRGLKYLHSAGILHRDIKPGNLLVNSNC-----VLKICDFGLARVE-EPDESKHMTqevvtqyYRAPEILMGSRHYTS 184
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-255 1.76e-05

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: 46.56  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPSLed 129
Cdd:cd14173   10 LGEGAYARVQTCINLITNKEYAVKIiekRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSI-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKEYIDPETHKHIPYR 208
Cdd:cd14173   88 LSHIHRRRhFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILC--EHPNQVSPVKICDFDLGSGIKLNSDCSPISTP 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 209 EHKSLTGTARYMS--INTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14173  166 ELLTPCGSAEYMApeVVEAFNEEASiydKRCDLWSLGVILYIMLSGYPPFVG 217
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
146-198 1.77e-05

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: 46.26  E-value: 1.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919096895 146 IAIQLVTRMEYVHSK-HLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYID 198
Cdd:cd06617  108 IAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVK-----LCDFGISGYLVD 156
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
118-287 1.81e-05

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: 46.44  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL-GPSLE-DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd05607   79 LVMSLMnGGDLKyHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCR-----LSDLGLAVE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 196 yidpethkhipYREHKSLT---GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKEryqkigDTK 272
Cdd:cd05607  154 -----------VKEGKPITqraGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKE------ELK 216
                        170
                 ....*....|....*...
gi 919096895 273 RAT-PIEVLCE--NFPEE 287
Cdd:cd05607  217 RRTlEDEVKFEhqNFTEE 234
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
47-207 1.89e-05

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: 46.04  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRA-PQLHLEYRFYKQLGQSEgVPQVYYFGPCGKYNALVLELLgp 125
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTrARAFQERDILARLSHRR-LTCLLDQFETRKTLILILELC-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHIIYIIDFGLAKEyIDPETHK 203
Cdd:cd14107   81 SSEELLDRLFLKGVVteAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM---VSPTREDIKICDFGFAQE-ITPSEHQ 156

                 ....
gi 919096895 204 HIPY 207
Cdd:cd14107  157 FSKY 160
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
147-268 1.89e-05

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: 46.41  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 147 AIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPEThkhipyrEHKSLTGTARYMSINTHL 226
Cdd:cd05608  111 TAQIISGLEHLHQRRIIYRDLKPENVLLDDDGN-----VRISDLGLAVELKDGQT-------KTKGYAGTPGFMAPELLL 178
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919096895 227 GKEQSRRDDLEALGHMFMYFL--RGSLPWQGLKADTlKERYQKI 268
Cdd:cd05608  179 GEEYDYSVDYFTLGVTLYEMIaaRGPFRARGEKVEN-KELKQRI 221
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
46-195 2.04e-05

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: 46.32  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELR------LGKNLYNNEhVAIKLEPMKSRAPQ---LHLEYRFYKQLGQSEGVpqVYYFGPCGKYN 116
Cdd:cd05055   36 NLSFGKTLGAGAFGKVVeataygLSKSDAVMK-VAVKMLKPTAHSSEreaLMSELKIMSHLGNHENI--VNLLGACTIGG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSLEDLFDLCDRK----FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGL 192
Cdd:cd05055  113 PILVITEYCCYGDLLNFLRRKresfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-----THGKIVKICDFGL 187

                 ...
gi 919096895 193 AKE 195
Cdd:cd05055  188 ARD 190
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
143-257 2.12e-05

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: 46.22  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 143 VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyidpethKHIPYREHKSLTGTARYMSI 222
Cdd:cd07869  105 VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELK-----LADFGLARA-------KSVPSHTYSNEVVTLWYRPP 172
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 919096895 223 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLK 257
Cdd:cd07869  173 DVLLGStEYSTCLDMWGVGCIFVEMIQGVAAFPGMK 208
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
156-254 2.15e-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: 46.05  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 156 YVHSKHLIYRDVKPENFLIGRQSAKkqhiiyIIDFGLAKEyIDPEThKHIpYREHKSltGTARYMS------INTHLGKE 229
Cdd:cd14131  118 TIHEEGIVHSDLKPANFLLVKGRLK------LIDFGIAKA-IQNDT-TSI-VRDSQV--GTLNYMSpeaikdTSASGEGK 186
                         90       100
                 ....*....|....*....|....*....
gi 919096895 230 Q----SRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14131  187 PkskiGRPSDVWSLGCILYQMVYGKTPFQ 215
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
138-254 2.49e-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: 46.21  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 138 FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETHKHIpyrehksltGTA 217
Cdd:cd05633  105 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVR-----ISDLGLACDFSKKKPHASV---------GTH 170
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919096895 218 RYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd05633  171 GYMAPEVlQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
52-194 2.51e-05

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: 45.88  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSRAPQ--LHLEYRFYKQLGQSEGVPQVYYFGPCGKYNaLVLELLGPSL 127
Cdd:cd07846    8 LVGEGSYGMVMKCRHKETGQIVAIKkfLESEDDKMVKkiAMREIKMLKQLRHENLVNLIEVFRRKKRWY-LVFEFVDHTV 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAK 194
Cdd:cd07846   87 LDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSG-----VVKLCDFGFAR 148
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
146-220 2.51e-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: 46.16  E-value: 2.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 146 IAiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYidPETHKHIPYREHkSLTGTARYM 220
Cdd:cd05598  107 IA-ELVCAIESVHKMGFIHRDIKPDNILIDRDG----H-IKLTDFGLCTGF--RWTHDSKYYLAH-SLVGTPNYI 172
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
52-224 2.54e-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: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK-----LEPmKSRApQLHLEYRFYKQLGQ-----SEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd14038    1 RLGTGGFGNVLRWINQETGEQVAIKqcrqeLSP-KNRE-RWCLEIQIMKRLNHpnvvaARDVPEGLQKLAPNDLPLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LL-GPSLEDLFDLCDRKFSLK--TVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKE--- 195
Cdd:cd14038   79 YCqGGDLRKYLNQFENCCGLRegAILTLLSDISSALRYLHENRIIHRDLKPENIVL--QQGEQRLIHKIIDLGYAKEldq 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 919096895 196 ------------YIDPEthkhipYREHKSLTGTARYMSINT 224
Cdd:cd14038  157 gslctsfvgtlqYLAPE------LLEQQKYTVTVDYWSFGT 191
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-207 2.58e-05

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: 45.79  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMKS---RAPQLHLEYRFYKQLGQSEGVP--QVYyfgPCGKYNALVLELLgpSL 127
Cdd:cd14167   11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlegKETSIENEIAVLHKIKHPNIVAldDIY---ESGGHLYLIMQLV--SG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAK----------- 194
Cdd:cd14167   86 GELFDRIVEKgfYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLY--YSLDEDSKIMISDFGLSKiegsgsvmsta 163
                        170
                 ....*....|....*..
gi 919096895 195 ----EYIDPETHKHIPY 207
Cdd:cd14167  164 cgtpGYVAPEVLAQKPY 180
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
118-202 2.68e-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: 45.82  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYI 197
Cdd:cd07845   85 LVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG-----CLKIADFGLARTYG 159

                 ....*
gi 919096895 198 DPETH 202
Cdd:cd07845  160 LPAKP 164
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
150-254 2.69e-05

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: 45.60  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 150 LVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQhiIYIIDFGLAkeyidpETHKHIPYREHKSLTGTARYMSINTHLGKE 229
Cdd:cd14087  106 VLDGVKYLHGLGITHRDLKPENLLYYHPGPDSK--IMITDFGLA------STRKKGPNCLMKTTCGTPEYIAPEILLRKP 177
                         90       100
                 ....*....|....*....|....*
gi 919096895 230 QSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14087  178 YTQSVDMWAVGVIAYILLSGTMPFD 202
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
144-195 2.73e-05

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: 45.83  E-value: 2.73e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 144 LMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKE 195
Cdd:cd05048  127 LHIAIQIAAGMEYLSSHHYVHRDLAARNCLVG-----DGLTVKISDFGLSRD 173
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
50-277 2.83e-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: 45.45  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEyrfyKQLGQSEGVPQ-------------VYYFG--PCGK 114
Cdd:cd06629    6 GELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADS----RQKTVVDALKSeidtlkdldhpniVQYLGfeETED 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YNALVLELL-GPSLEDlfdlCDRK---FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDF 190
Cdd:cd06629   82 YFSIFLEYVpGGSIGS----CLRKygkFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICK-----ISDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 191 GLAKEyidpetHKHIpYREHK--SLTGTARYMS---INThLGKEQSRRDDLEALGHMFMYFLRGSLPWqglkadTLKERY 265
Cdd:cd06629  153 GISKK------SDDI-YGNNGatSMQGSVFWMApevIHS-QGQGYSAKVDIWSLGCVVLEMLAGRRPW------SDDEAI 218
                        250
                 ....*....|....*
gi 919096895 266 Q---KIGDTKRATPI 277
Cdd:cd06629  219 AamfKLGNKRSAPPV 233
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
135-252 2.96e-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: 45.37  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKEYIDP---ETHKHIPYREHK 211
Cdd:cd14172   97 DQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLY--TSKEKDAVLKLTDFGFAKETTVQnalQTPCYTPYYVAP 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 919096895 212 SLTGTARYmsinthlgkeqSRRDDLEALGhMFMYFLRGSLP 252
Cdd:cd14172  175 EVLGPEKY-----------DKSCDMWSLG-VIMYILLCGFP 203
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
47-267 3.06e-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: 45.62  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQL---------HLEYRFYKQLGQSEGVPQVYYfgpcgk 114
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKinrEKAGSSAVKLlerevdilkHVNHAHIIHLEEVFETPKRMY------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 ynaLVLELL-GPSLEDLFDlcdRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQH--IIYIID 189
Cdd:cd14097   77 ---LVMELCeDGELKELLL---RKgfFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNDklNIKVTD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 190 FGLA-KEYIDPETHkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 267
Cdd:cd14097  151 FGLSvQKYGLGEDM-------LQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK 222
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
51-315 3.21e-05

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: 45.29  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGknLYN-NEHVAIKLEPMKSRAPQLHL-EYRFYKQLGQSEGVPQVYYFGPCGKYnaLVLELL--GPS 126
Cdd:cd14203    1 VKLGQGCFGEVWMG--TWNgTTKVAIKTLKPGTMSPEAFLeEAQIMKKLRHDKLVQLYAVVSEEPIY--IVTEFMskGSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEthkhip 206
Cdd:cd14203   77 LDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCK-----IADFGLARLIEDNE------ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 207 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLKADTLKERYQKigdtKRATPIEVLCenfP 285
Cdd:cd14203  146 YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMNNREVLEQVER----GYRMPCPPGC---P 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 919096895 286 EELATYLRYVRRLDFFETPDYDYLRKLFTD 315
Cdd:cd14203  219 ESLHELMCQCWRKDPEERPTFEYLQSFLED 248
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
51-219 3.25e-05

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: 45.60  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHL-EYRFYKQLGQS--------------EGVPQVYyfgpc 112
Cdd:cd07837    7 EKIGEGTYGKVYKARDKNTGKLVALKktrLEMEEEGVPSTALrEVSLLQMLSQSiyivrlldvehveeNGKPLLY----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 gkynaLVLELLGPSLEDLFDLCDR----KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHIIYII 188
Cdd:cd07837   82 -----LVFEYLDTDLKKFIDSYGRgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVD----KQKGLLKIA 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 919096895 189 DFGLAKEYIDP---ETHKHIP--YREHKSLTGTARY 219
Cdd:cd07837  153 DLGLGRAFTIPiksYTHEIVTlwYRAPEVLLGSTHY 188
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
113-195 3.26e-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: 45.70  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 GKYNALVLELL-GpslEDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQHiIYIID 189
Cdd:cd14091   66 GNSVYLVTELLrG---GELLDriLRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPES-LRICD 141

                 ....*.
gi 919096895 190 FGLAKE 195
Cdd:cd14091  142 FGFAKQ 147
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
51-265 3.29e-05

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: 45.48  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRaPQLHLEYRFYKQLGQSEGVPQVYYFGP--CGKYNALVLELL-GPSL 127
Cdd:cd06656   25 EKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQ-PKKELIINEILVMRENKNPNIVNYLDSylVGDELWVVMEYLaGGSL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLF-DLCDRKFSLKTVLMIAIQlvtRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyIDPETHKhip 206
Cdd:cd06656  104 TDVVtETCMDEGQIAAVCRECLQ---ALDFLHSNQVIHRDIKSDNILLGMDGSVK-----LTDFGFCAQ-ITPEQSK--- 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 207 yreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 265
Cdd:cd06656  172 ---RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALY 225
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
118-287 3.76e-05

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: 45.43  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL--GPSLEDLfdlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd14118   93 MVFELVdkGAVMEVP---TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVK-----IADFGVSNE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 196 Y--IDPEThkhipyrehKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIgd 270
Cdd:cd14118  165 FegDDALL---------SSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFE---DDHILGLHEKI-- 230
                        170
                 ....*....|....*..
gi 919096895 271 tkRATPIEvlcenFPEE 287
Cdd:cd14118  231 --KTDPVV-----FPDD 240
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
27-259 3.91e-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: 45.38  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  27 GMHSNRTSSSGSGVLMVGPNFRVGKKIGCGNFGE-LRLGKNLYN-NEHVAIKLEPMKSRApQLHLEYRFYKQLgqsEGVP 104
Cdd:cd14207   68 GHHLNVVNLLGACTKSGGPLMVIVEYCKYGNLSNyLKSKRDFFVtNKDTSLQEELIKEKK-EAEPTGGKKKRL---ESVT 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 105 QVYYFGPCGKYNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHI 184
Cdd:cd14207  144 SSESFASSGFQEDKSLSDVEEEEEDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILL-----SENNV 218
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 185 IYIIDFGLAKE-YIDPEthkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKAD 259
Cdd:cd14207  219 VKICDFGLARDiYKNPD------YVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGvLLWEIFSLGASPYPGVQID 289
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
129-253 3.93e-05

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: 45.35  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAkeyidpethKHI- 205
Cdd:cd14181  102 ELFDYLTEKVTLseKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL-----DDQLHIKLSDFGFS---------CHLe 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 206 PYREHKSLTGTARYMSI--------NTH--LGKEQsrrdDLEALGHMFMYFLRGSLPW 253
Cdd:cd14181  168 PGEKLRELCGTPGYLAPeilkcsmdETHpgYGKEV----DLWACGVILFTLLAGSPPF 221
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
135-253 4.10e-05

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: 45.41  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHS-KHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYI-DPEThkhipyreHKS 212
Cdd:cd05594  119 ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-----IKITDFGLCKEGIkDGAT--------MKT 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 919096895 213 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05594  186 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 226
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
51-194 4.18e-05

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 45.09  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGknLYNNE-HVAIKLEPMKSRAPQLHL-EYRFYKQLGQSEGVpQVYYFGPCGKYNALVLELLG-PSL 127
Cdd:cd05068   14 RKLGSGQFGEVWEG--LWNNTtPVAVKTLKPGTMDPEDFLrEAQIMKKLRHPKLI-QLYAVCTLEEPIYIITELMKhGSL 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAK 194
Cdd:cd05068   91 LEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENN-----ICKVADFGLAR 152
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
47-202 4.18e-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: 44.87  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLG--KNLYNNEHVAIKLEPmKSRAPQLHLEyRFY-------KQLgQSEGVPQVY-YFGPCGKYn 116
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIID-KKKAPKDFLE-KFLpreleilRKL-RHPNIIQVYsIFERGSKV- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSleDLFDLCDRKFSL---KTVLMIAiQLVTRMEYVHSKHLIYRDVKPENFLIgrqsAKKQHiIYIIDFGLA 193
Cdd:cd14080   78 FIFMEYAEHG--DLLEYIQKRGALsesQARIWFR-QLALAVQYLHSLDIAHRDLKCENILL----DSNNN-VKLSDFGFA 149

                 ....*....
gi 919096895 194 KEYIDPETH 202
Cdd:cd14080  150 RLCPDDDGD 158
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
49-261 4.33e-05

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: 45.39  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKNL-----YNNEHVAIKLEPMKSRAPQLHL-----EYRFYKQLGQSEGVpqVYYFGPCGKYNAL 118
Cdd:cd05101   28 LGKPLGEGCFGQVVMAEAVgidkdKPKEAVTVAVKMLKDDATEKDLsdlvsEMEMMKMIGKHKNI--INLLGACTQDGPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 --VLELLG-------------PSLEDLFDLC---DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaK 180
Cdd:cd05101  106 yvIVEYASkgnlreylrarrpPGMEYSYDINrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV-----T 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 181 KQHIIYIIDFGLAK-----EYIDPETHKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQ 254
Cdd:cd05101  181 ENNVMKIADFGLARdinniDYYKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLMWEIFTLGGSPYP 250

                 ....*..
gi 919096895 255 GLKADTL 261
Cdd:cd05101  251 GIPVEEL 257
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
146-253 4.34e-05

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: 45.25  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEThkhipyrehKSLTGTARYMSINTH 225
Cdd:cd06619  100 IAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVK-----LCDFGVSTQLVNSIA---------KTYVGTNAYMAPERI 165
                         90       100
                 ....*....|....*....|....*...
gi 919096895 226 LGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06619  166 SGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
51-193 4.56e-05

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: 45.01  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKnlYNNEhVAIKLEPMKSRAPQLHLEYRFYKQ-LGQSEGVPQVYYFGPCGKYN-ALVLELL-GPSL 127
Cdd:cd14150    6 KRIGTGSFGTVFRGK--WHGD-VAVKILKVTEPTPEQLQAFKNEMQvLRKTRHVNILLFMGFMTRPNfAIITQWCeGSSL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd14150   83 YRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVK-----IGDFGLA 143
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
47-196 4.91e-05

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: 44.96  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL--------------------------EPMKSRAP--QLHLEYRFYKQLG 98
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVlskkklmrqagfprrppprgaraapeGCTQPRGPieRVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  99 QSEGVPQVYYFG-PCGKYNALVLELL--GPSLEDLfdlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIG 175
Cdd:cd14199   84 HPNVVKLVEVLDdPSEDHLYMVFELVkqGPVMEVP---TLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG 160
                        170       180
                 ....*....|....*....|.
gi 919096895 176 RQSAkkqhiIYIIDFGLAKEY 196
Cdd:cd14199  161 EDGH-----IKIADFGVSNEF 176
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
47-208 4.92e-05

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: 44.69  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHL--EYRFYKQLgQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSikkDKIEDEQDMVRIrrEIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 122 LlgPSLEDLFDLCDRKFSL--KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEYID- 198
Cdd:cd14073   82 Y--ASGGELYDYISERRRLpeREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL-----DQNGNAKIADFGLSNLYSKd 154
                        170       180
                 ....*....|....*....|....
gi 919096895 199 --------------PETHKHIPYR 208
Cdd:cd14073  155 kllqtfcgsplyasPEIVNGTPYQ 178
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
53-253 5.02e-05

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: 44.71  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAP-----QLHLEYRFYKQLGQSeGVPQVYYFGPCGKYNALVLELL-GPS 126
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVID-KLRFPtkqesQLRNEVAILQQLSHP-GVVNLECMFETPERVFVVMEKLhGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 127 LEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQhiIYIIDFGLAKeyIDPETHkhip 206
Cdd:cd14082   89 LEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQ--VKLCDFGFAR--IIGEKS---- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 919096895 207 YRehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd14082  161 FR--RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 205
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
51-276 5.62e-05

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 44.57  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLG--KNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQ-VYYFGPC-GKYNALVLEL--LG 124
Cdd:cd05116    1 GELGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYiVRMIGICeAESWMLVMEMaeLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSleDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK------EYID 198
Cdd:cd05116   81 PL--NKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL-----VTQHYAKISDFGLSKalradeNYYK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 199 PETHKHIPYREHKSltgtaryMSINTHlgkEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLK---ERYQKIGDTKRA 274
Cdd:cd05116  154 AQTHGKWPVKWYAP-------ECMNYY---KFSSKSDVWSFGvLMWEAFSYGQKPYKGMKGNEVTqmiEKGERMECPAGC 223

                 ..
gi 919096895 275 TP 276
Cdd:cd05116  224 PP 225
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-252 6.36e-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: 44.66  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKH-LIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHkhipyrehkSLTGTARYMSINT 224
Cdd:cd06650  108 VSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMAN---------SFVGTRSYMSPER 173
                         90       100
                 ....*....|....*....|....*...
gi 919096895 225 HLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06650  174 LQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
51-209 6.85e-05

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: 44.62  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGK--NLYNN--EHVAIKlEPMKSRAPQL---HLEYRFYKQLgQSEGVpqVYYFGPC---GKYN-ALV 119
Cdd:cd14205   10 QQLGKGNFGSVEMCRydPLQDNtgEVVAVK-KLQHSTEEHLrdfEREIEILKSL-QHDNI--VKYKGVCysaGRRNlRLI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELLgP--SLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeyI 197
Cdd:cd14205   86 MEYL-PygSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVK-----IGDFGLTK--V 157
                        170
                 ....*....|..
gi 919096895 198 DPETHKHIPYRE 209
Cdd:cd14205  158 LPQDKEYYKVKE 169
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
49-261 6.88e-05

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: 44.62  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKNLYNNEH-------VAIKLepMKSRAPQLHL-----EYRFYKQLGQSEGVpqVYYFGPCGKYN 116
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAIGLDKDkpnrvtkVAVKM--LKSDATEKDLsdlisEMEMMKMIGKHKNI--INLLGACTQDG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 AL--VLELLG-------------PSLEDLFD---LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqs 178
Cdd:cd05098   93 PLyvIVEYASkgnlreylqarrpPGMEYCYNpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV---- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 179 aKKQHIIYIIDFGLAKEYidpethKHIPYREhKSLTG--TARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQG 255
Cdd:cd05098  169 -TEDNVMKIADFGLARDI------HHIDYYK-KTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGvLLWEIFTLGGSPYPG 240

                 ....*.
gi 919096895 256 LKADTL 261
Cdd:cd05098  241 VPVEEL 246
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
51-252 6.96e-05

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: 44.66  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNAL--VLELLGP-SL 127
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLwiIMEYLGGgSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDL-----FDlcdrKFSLKTVLMiaiQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETH 202
Cdd:cd06640   90 LDLlragpFD----EFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVK-----LADFGVAGQLTDTQIK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06640  158 R-------NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-255 7.00e-05

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: 44.64  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMK---SRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPSLed 129
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSI-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRK-FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKEYIDPETHKHIPYR 208
Cdd:cd14174   88 LAHIQKRKhFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILC--ESPDKVSPVKICDFDLGSGVKLNSACTPITTP 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 209 EHKSLTGTARYMS-----INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14174  166 ELTTPCGSAEYMApevveVFTDEATFYDKRCDLWSLGVILYIMLSGYPPFVG 217
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
125-261 7.02e-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: 44.57  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSLEDLFD---LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK-----EY 196
Cdd:cd05099  115 PGPDYTFDitkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMK-----IADFGLARgvhdiDY 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 197 IDPETHKHIPYrehKSLTGTARYMSINTHlgkeQSRRDDLEALghMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05099  190 YKKTSNGRLPV---KWMAPEALFDRVYTH----QSDVWSFGIL--MWEIFTLGGSPYPGIPVEEL 245
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
149-221 7.23e-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: 44.34  E-value: 7.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGrqSAKKQHIIYIIDFGLAKEYIDPETHKHipyrehkSLTGTARYMS 221
Cdd:cd14086  108 QILESVNHCHQNGIVHRDLKPENLLLA--SKSKGAAVKLADFGLAIEVQGDQQAWF-------GFAGTPGYLS 171
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
145-270 7.87e-05

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: 44.32  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 145 MIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsAKKQHiIYIIDFGLAK------------EYIDPETHKHIpyreHKS 212
Cdd:cd05609  104 MYFAETVLALEYLHSYGIVHRDLKPDNLLI----TSMGH-IKLTDFGLSKiglmslttnlyeGHIEKDTREFL----DKQ 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 213 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERY-QKIGD 270
Cdd:cd05609  175 VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEELFgQVISD 230
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
135-253 7.98e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 44.59  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKeYIDPETHkhipyrehkSLT 214
Cdd:PTZ00426 125 NKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL-----DKDGFIKMTDFGFAK-VVDTRTY---------TLC 189
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 919096895 215 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:PTZ00426 190 GTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
146-193 8.36e-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: 44.47  E-value: 8.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA 193
Cdd:cd07852  112 IMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVK-----LADFGLA 154
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
134-194 8.41e-05

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: 43.95  E-value: 8.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 134 CDRKFSLKTVLM-IAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAK 194
Cdd:cd05052   96 CNREELNAVVLLyMATQIASAMEYLEKKNFIHRDLAARNCLVG-----ENHLVKVADFGLSR 152
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
47-253 8.51e-05

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 44.21  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQ------LHLEYRFYKQLGQsEGVPQVYYF--GPCGKYnAL 118
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIID-KSGGPEefiqrfLPRELQIVERLDH-KNIIHVYEMleSADGKI-YL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELLGPSleDLFDLCDRKFSLKTVLMIAI--QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiiyIIDFGLAKEY 196
Cdd:cd14163   79 VMELAEDG--DVFDCVLHGGPLPEHRAKALfrQLVEAIRYCHGCGVAHRDLKCENALLQGFTLK------LTDFGFAKQL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 197 idPETHKHIPyrehKSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd14163  151 --PKGGRELS----QTFCGSTAYAAPEVLQGvPHDSRKGDIWSMGVVLYVMLCAQLPF 202
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
52-220 8.58e-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: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQLgQSEGVpqVYYFGPCGKYNAL--VLELL-GP 125
Cdd:cd06610    8 VIGSGATAVVYAAYCLPKKEKVAIKridLEKCQTSMDELRKEIQAMSQC-NHPNV--VSYYTSFVVGDELwlVMPLLsGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLedlFDLCDRKFSLKTVLMIAIQLVTR-----MEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPE 200
Cdd:cd06610   85 SL---LDIMKSSYPRGGLDEAIIATVLKevlkgLEYLHSNGQIHRDVKAGNILLGEDGSVK-----IADFGVSASLATGG 156
                        170       180
                 ....*....|....*....|
gi 919096895 201 THKHipyREHKSLTGTARYM 220
Cdd:cd06610  157 DRTR---KVRKTFVGTPCWM 173
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
145-203 8.67e-05

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: 44.38  E-value: 8.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 145 MIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQsakkQHIIYIIDFGLAKeYIDPE-THK 203
Cdd:cd07854  118 LFMYQLLRGLKYIHSANVLHRDLKPANVFINTE----DLVLKIGDFGLAR-IVDPHySHK 172
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
129-194 8.81e-05

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: 44.15  E-value: 8.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRK----FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgRQSAkkqHIIyIIDFGLAK 194
Cdd:cd05574   87 ELFRLLQKQpgkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILL-HESG---HIM-LTDFDLSK 151
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
47-279 8.97e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 45.11  E-value: 8.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895   47 FRVGKKIGCGNFGELRLGKNLYNNEHV---AIKLEPMKSR-APQLHLEYRFYKQLGQSEGVpqvyyfgpcgKYNALVLEL 122
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFcwkAISYRGLKEReKSQLVIEVNVMRELKHKNIV----------RYIDRFLNK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  123 LGPSLEDLFDLCDR---------------KFSLKTVLMIAIQLVTRMEYVHS-------KHLIYRDVKPEN-FL------ 173
Cdd:PTZ00266   85 ANQKLYILMEFCDAgdlsrniqkcykmfgKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNiFLstgirh 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  174 IGRQSAKKQH-----IIYIIDFGLAKEyIDPETHKHipyrehkSLTGTARYMS--INTHLGKEQSRRDDLEALGHMFMYF 246
Cdd:PTZ00266  165 IGKITAQANNlngrpIAKIGDFGLSKN-IGIESMAH-------SCVGTPYYWSpeLLLHETKSYDDKSDMWALGCIIYEL 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 919096895  247 LRGSLPWQglKADTLKeryQKIGDTKRATPIEV 279
Cdd:PTZ00266  237 CSGKTPFH--KANNFS---QLISELKRGPDLPI 264
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
129-255 9.73e-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: 43.75  E-value: 9.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFD-LCDRKFSLKTV--LMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqHIIYIIDFGLAKEYiDPETHKHI 205
Cdd:cd14190   87 ELFErIVDEDYHLTEVdaMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTG---HQVKIIDFGLARRY-NPREKLKV 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 206 PYrehksltGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14190  163 NF-------GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLG 205
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
137-276 9.80e-05

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: 44.22  E-value: 9.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYI-DPEThkhipyreHKSLTG 215
Cdd:cd05616   97 RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH-----IKIADFGMCKENIwDGVT--------TKTFCG 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 216 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkerYQKIGDTKRATP 276
Cdd:cd05616  164 TPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDEL---FQSIMEHNVAYP 221
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
52-253 1.06e-04

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: 43.87  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNlynNEHVAIKLEPMKSRAPQLHLEYRF-YKQLGQSEGVPQVYYFGPCGKYN-ALVLELL-GPSLE 128
Cdd:cd14149   19 RIGSGSFGTVYKGKW---HGDVAVKILKVVDPTPEQFQAFRNeVAVLRKTRHVNILLFMGYMTKDNlAIVTQWCeGSSLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 129 DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETHKHIpyr 208
Cdd:cd14149   96 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK-----IGDFGLATVKSRWSGSQQV--- 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 209 ehKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd14149  168 --EQPTGSILWMApevIRMQDNNPFSFQSDVYSYGIVLYELMTGELPY 213
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-240 1.06e-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: 44.00  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK---LEPMKSRAPQLHLEYRFYKQL--GQSEGVPQVYyfgpcGKYnalvleLLGPSL 127
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKvlnLDTDDDDVSDIQKEVALLSQLklGQPKNIIKYY-----GSY------LKGPSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCDRKfSLKTvLMIA-------IQLVTR-----MEYVHSKHLIYRDVKPENFLIGRqsakkQHIIYIIDFGLAKE 195
Cdd:cd06917   78 WIIMDYCEGG-SIRT-LMRAgpiaeryIAVIMRevlvaLKFIHKDGIIHRDIKAANILVTN-----TGNVKLCDFGVAAS 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 919096895 196 YidpethkHIPYREHKSLTGTARYMSINTHL-GKEQSRRDDLEALG 240
Cdd:cd06917  151 L-------NQNSSKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLG 189
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
53-193 1.06e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 44.25  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEY--RFYKQLGQSEGVPQVYYFGPCGKYNALVLELLGPSL 127
Cdd:cd14229    8 LGRGTFGQVVKCWKRGTNEIVAVKIlknHPSYARQGQIEVGIlaRLSNENADEFNFVRAYECFQHRNHTCLVFEMLEQNL 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 128 EDLfdLCDRKFS---LKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgRQSAKKQHIIYIIDFGLA 193
Cdd:cd14229   88 YDF--LKQNKFSplpLKVIRPILQQVATALKKLKSLGLIHADLKPENIML-VDPVRQPYRVKVIDFGSA 153
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
149-255 1.09e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 44.62  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPEN-FLIgrqsakKQHIIYIIDFGLAKEYIDPethkhIPYREHKSLTGTARYMSINTHLG 227
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANiFLM------PTGIIKLGDFGFSKQYSDS-----VSLDVASSFCGTPYYLAPELWER 245
                         90       100
                 ....*....|....*....|....*...
gi 919096895 228 KEQSRRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:PTZ00267 246 KRYSKKADMWSLGVILYELLTLHRPFKG 273
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
46-195 1.28e-04

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 43.83  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVY-YFGPCGKYNA----LV 119
Cdd:cd06639   23 TWDIIETIGKGTYGKVYKVTNKKDGSLAAVKiLDPISDVDEEIEAEYNILRSLPNHPNVVKFYgMFYKADQYVGgqlwLV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 120 LELL-GPSLEDLFD---LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd06639  103 LELCnGGSVTELVKgllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVK-----LVDFGVSAQ 177
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
47-293 1.32e-04

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: 43.83  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGEL-----RLGKNLYNNEHVAIK-LEPMKSRAPQLHlEYRFYKQLgQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd05631    2 FRHYRVLGKGGFGEVcacqvRATGKMYACKKLEKKrIKKRKGEAMALN-EKRILEKV-NSRFVVSLAYAYETKDALCLVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 ELL-GPSLE-DLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsaKKQHiIYIIDFGLAKEYID 198
Cdd:cd05631   80 TIMnGGDLKfHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLD----DRGH-IRISDLGLAVQIPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 199 PEThkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYqkigDTKRATPIE 278
Cdd:cd05631  155 GET--------VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEV----DRRVKEDQE 222
                        250
                 ....*....|....*
gi 919096895 279 VLCENFPEELATYLR 293
Cdd:cd05631  223 EYSEKFSEDAKSICR 237
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
51-315 1.37e-04

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: 43.52  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGkNLYNNEHVAIKLEPMKSRAPQLHLE-YRFYKQLGQSEGVpQVYYFgPCGKYNALVLELL--GPSL 127
Cdd:cd05070   15 KRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTMSPESFLEeAQIMKKLKHDKLV-QLYAV-VSEEPIYIVTEYMskGSLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 128 EDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYIDPEthkhipY 207
Cdd:cd05070   92 DFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGL-----ICKIADFGLARLIEDNE------Y 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 208 REHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLKADTLKERYQKigDTKRATPievlcENFPE 286
Cdd:cd05070  161 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMNNREVLEQVER--GYRMPCP-----QDCPI 233
                        250       260
                 ....*....|....*....|....*....
gi 919096895 287 ELATYLRYVRRLDFFETPDYDYLRKLFTD 315
Cdd:cd05070  234 SLHELMIHCWKKDPEERPTFEYLQGFLED 262
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
130-267 1.42e-04

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: 43.81  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEyidpethkhIPYRE 209
Cdd:cd05632   93 IYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGH-----IRISDLGLAVK---------IPEGE 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 210 H-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 267
Cdd:cd05632  159 SiRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDR 217
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
50-221 1.49e-04

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 43.64  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  50 GKKIGCGNFGELRLGKnlYNNEHVAIK-LEPMKSRAPQlHLEYRFYKQLG-----QSEGVPQVYYFGPCGKYNALVLELL 123
Cdd:cd14158   20 GNKLGEGGFGVVFKGY--INDKNVAVKkLAAMVDISTE-DLTKQFEQEIQvmakcQHENLVELLGYSCDGPQLCLVYTYM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTR--MEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyiDPE 200
Cdd:cd14158   97 pNGSLLDRLACLNDTPPLSWHMRCKIAQGTAngINYLHENNHIHRDIKSANILLDETFVPK-----ISDFGLARA--SEK 169
                        170       180
                 ....*....|....*....|.
gi 919096895 201 THKHIPYREhksLTGTARYMS 221
Cdd:cd14158  170 FSQTIMTER---IVGTTAYMA 187
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
47-191 1.50e-04

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: 43.50  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGK---NLYNNEHVAIKLE-P----------------MKSRAPQLHLEYRfYKQLGQSEGVpQV 106
Cdd:cd13981    2 YVISKELGEGGYASVYLAKdddEQSDGSLVALKVEkPpsiwefyicdqlhsrlKNSRLRESISGAH-SAHLFQDESI-LV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 107 YYFGPCGkynalvlellgpSLEDLFDLCdRKFSLKT-----VLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGR-QSAK 180
Cdd:cd13981   80 MDYSSQG------------TLLDVVNKM-KNKTGGGmdeplAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLeICAD 146
                        170       180
                 ....*....|....*....|
gi 919096895 181 KQHI---------IYIIDFG 191
Cdd:cd13981  147 WPGEgengwlskgLKLIDFG 166
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
147-293 1.50e-04

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: 43.15  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 147 AIQLVTRMEYVHSKH---LIYRDVKPENFLIGRQSAKK---QHIIYIIDFGLAKEYidpethkhipYREHK-SLTGTARY 219
Cdd:cd14061   98 AIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEdleNKTLKITDFGLAREW----------HKTTRmSAAGTYAW 167
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 220 MS---INTHLgkeQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLCenfPEELATYLR 293
Cdd:cd14061  168 MApevIKSST---FSKASDVWSYGVLLWELLTGEVPYKGI--DGLAVAY-GVAVNKLTLPIPSTC---PEPFAQLMK 235
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
137-208 1.58e-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: 43.56  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGrqsakKQHIIYIIDFGLAKE--YID---PETHKHIPYR 208
Cdd:cd05053  129 QLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVT-----EDNVMKIADFGLARDihHIDyyrKTTNGRLPVK 200
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
149-253 1.67e-04

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: 43.27  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLI---GRQSAkkqhiiyIIDFGLAkEYIDPE-------THKHIPyrehksltGTAR 218
Cdd:cd13991  106 QALEGLEYLHSRKILHGDVKADNVLLssdGSDAF-------LCDFGHA-ECLDPDglgkslfTGDYIP--------GTET 169
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 919096895 219 YMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd13991  170 HMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
118-257 1.75e-04

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: 43.32  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSleDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakKQHIIYIIDFGLAKE 195
Cdd:cd14180   78 LVMELLRGG--ELLDRIKKKarFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADES--DGAVLKVIDFGFARL 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 196 YIDPETHKHIPyrehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 257
Cdd:cd14180  154 RPQGSRPLQTP-------CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKR 208
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
48-261 1.78e-04

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 43.14  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  48 RVGKKIGCGNFGELRlgKNLYNNEHVAIK-LEPM-KSRAPQ---------LHLEYR-FYKQLGQSEGVPQvyyfgpcGKY 115
Cdd:cd13979    6 RLQEPLGSGGFGSVY--KATYKGETVAVKiVRRRrKNRASRqsfwaelnaARLRHEnIVRVLAAETGTDF-------ASL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 116 NALVLELLG-PSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd13979   77 GLIIMEYCGnGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCK-----LCDFGCSV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 195 EYIDP-ETHKHIPYrehksLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 261
Cdd:cd13979  152 KLGEGnEVGTPRSH-----IGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVL 214
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
51-264 1.81e-04

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: 43.15  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPmKSRAPQLHLE--YR---FYKQLGQSEgVPQVYYFGPCGKYNALVLELlgP 125
Cdd:cd14071    6 RTIGKGNFAVVKLARHRITKTEVAIKIID-KSQLDEENLKkiYRevqIMKMLNHPH-IIKLYQVMETKDMLYLVTEY--A 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLFDLCDR--KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPEThk 203
Cdd:cd14071   82 SNGEIFDYLAQhgRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN-----IKIADFGFSNFFKPGEL-- 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 204 hipyreHKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 264
Cdd:cd14071  155 ------LKTWCGSPPYAAPEVFEGKEYEGPQlDIWSLGVVLYVLVCGALPFDGSTLQTLRDR 210
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
125-261 1.92e-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: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 125 PSLEDLFDLC---DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK-----EY 196
Cdd:cd05100  115 PGMDYSFDTCklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV-----TEDNVMKIADFGLARdvhniDY 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 197 IDPETHKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05100  190 YKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLLWEIFTLGGSPYPGIPVEEL 245
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
53-195 2.01e-04

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 43.08  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQSEGVpqVYYFGPCGKYNA-------LVLELL- 123
Cdd:cd06638   26 IGKGTYGKVFKVLNKKNGSKAAVKiLDPIHDIDEEIEAEYNILKALSDHPNV--VKFYGMYYKKDVkngdqlwLVLELCn 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 124 GPSLEDLFDLCDRKFSLKTVLMIAIQL---VTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd06638  104 GGSVTDLVKGFLKRGERMEEPIIAYILheaLMGLQHLHVNKTIHRDVKGNNILLTTEGGVK-----LVDFGVSAQ 173
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-212 2.16e-04

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 43.08  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLepMKSRAP---QLHLEYRFYKQLGQsegvpqvyyFGPCGKYN------------- 116
Cdd:cd14226   21 IGKGSFGQVVKAYDHVEQEWVAIKI--IKNKKAflnQAQIEVRLLELMNK---------HDTENKYYivrlkrhfmfrnh 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 -ALVLELLGPSLEDL-----FdlcdRKFSLKTVLMIAIQLVTRMEYVHSKHL--IYRDVKPENFLIgrQSAKKQHiIYII 188
Cdd:cd14226   90 lCLVFELLSYNLYDLlrntnF----RGVSLNLTRKFAQQLCTALLFLSTPELsiIHCDLKPENILL--CNPKRSA-IKII 162
                        170       180
                 ....*....|....*....|....
gi 919096895 189 DFGlAKEYIDPETHKHIPYREHKS 212
Cdd:cd14226  163 DFG-SSCQLGQRIYQYIQSRFYRS 185
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
53-203 2.23e-04

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: 42.85  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQsegvPQVYYF-GPC---GKYNALVLELLGPSLE 128
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREVQLMNRLSH----PNILRFmGVCvhqGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 129 DLFDlCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQsaKKQHIIYIIDFGLAKEYIDPETHK 203
Cdd:cd14155   77 QLLD-SNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRD--ENGYTAVVGDFGLAEKIPDYSDGK 148
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
79-273 2.32e-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: 43.04  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  79 PMKSRAPQLHLEYRFYKQLGQS-----EGVPQVYYFGPCGKYNAlvlellgPSLEDLFDLCDRKFSLKTVLMIAIQLVTR 153
Cdd:cd05102  112 PYRERSPRTRSQVRSMVEAVRAdrrsrQGSDRVASFTESTSSTN-------QPRQEVDDLWQSPLTMEDLICYSFQVARG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 154 MEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKE-YIDPEthkhipYREHKSLTGTARYMSINTHLGKEQSR 232
Cdd:cd05102  185 MEFLASRKCIHRDLAARNILL-----SENNVVKICDFGLARDiYKDPD------YVRKGSARLPLKWMAPESIFDKVYTT 253
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 919096895 233 RDDLEALG-HMFMYFLRGSLPWQGLKADtlKERYQKIGDTKR 273
Cdd:cd05102  254 QSDVWSFGvLLWEIFSLGASPYPGVQIN--EEFCQRLKDGTR 293
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
113-254 2.41e-04

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: 42.86  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 113 GKYNALVLELL-GPSL-------EDLFDLCDRKFslktvLMIAIQLVTRMEYVHSKHLIYRDVKPENflIGRQSAKKQHI 184
Cdd:cd13988   65 TRHKVLVMELCpCGSLytvleepSNAYGLPESEF-----LIVLRDVVAGMNHLRENGIVHRDIKPGN--IMRVIGEDGQS 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 185 IY-IIDFGLAKEYIDPEthkhipyrEHKSLTGTARYMS--------INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd13988  138 VYkLTDFGAARELEDDE--------QFVSLYGTEEYLHpdmyeravLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
138-254 2.52e-04

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: 43.11  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 138 FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHKHIpyrehksltGTA 217
Cdd:cd14223  100 FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH-----VRISDLGLACDFSKKKPHASV---------GTH 165
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919096895 218 RYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 254
Cdd:cd14223  166 GYMAPEVlQKGVAYDSSADWFSLGCMLFKLLRGHSPFR 203
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
118-219 2.56e-04

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: 42.71  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELL--GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKE 195
Cdd:cd14170   76 IVMECLdgGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY--TSKRPNAILKLTDFGFAKE 153
                         90       100       110
                 ....*....|....*....|....*....|
gi 919096895 196 yidPETHK------HIPYREHKSLTGTARY 219
Cdd:cd14170  154 ---TTSHNslttpcYTPYYVAPEVLGPEKY 180
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
118-207 2.56e-04

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: 42.83  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSleDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakKQHIIYIIDFGLAKE 195
Cdd:cd14171   86 IVMELMEGG--ELFDRISQHrhFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNS--EDAPIKLCDFGFAKV 161
                         90
                 ....*....|...
gi 919096895 196 YI-DPETHKHIPY 207
Cdd:cd14171  162 DQgDLMTPQFTPY 174
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
154-224 2.69e-04

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: 42.60  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 154 MEYVHSKHLIYRDVKPENFLIGRQSAKKQHiiYIIDFGLAK---------------EYIDPETHkhipyrEHKSLTGTAR 218
Cdd:cd14039  112 IQYLHENKIIHRDLKPENIVLQEINGKIVH--KIIDLGYAKdldqgslctsfvgtlQYLAPELF------ENKSYTVTVD 183

                 ....*.
gi 919096895 219 YMSINT 224
Cdd:cd14039  184 YWSFGT 189
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
134-240 2.77e-04

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: 42.42  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 134 CDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPEN-FLigrqsaKKQHIIYIIDFGLAKEyIDPEthkhipYREHKS 212
Cdd:cd08221   94 KNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNiFL------TKADLVKLGDFGISKV-LDSE------SSMAES 160
                         90       100
                 ....*....|....*....|....*...
gi 919096895 213 LTGTARYMSINTHLGKEQSRRDDLEALG 240
Cdd:cd08221  161 IVGTPYYMSPELVQGVKYNFKSDIWAVG 188
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
142-240 2.98e-04

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 42.53  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 142 TVLMIAIQLVTRMEYVHSKH-----LIYRDVKPEN-FLIGRQSAKkqhiiyIIDFGLAKEYidpethkHIPYREHKSLTG 215
Cdd:cd08217  106 FIWKIFTQLLLALYECHNRSvgggkILHRDLKPANiFLDSDNNVK------LGDFGLARVL-------SHDSSFAKTYVG 172
                         90       100
                 ....*....|....*....|....*
gi 919096895 216 TARYMSINTHLGKEQSRRDDLEALG 240
Cdd:cd08217  173 TPYYMSPELLNEQSYDEKSDIWSLG 197
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
149-298 3.10e-04

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: 42.49  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHiIYIIDFGLA-----KEYIDPETHKHIPYREHKSLTGTARYMSIN 223
Cdd:cd14049  128 QLLEGVTYIHSMGIVHRDLKPRNIFL---HGSDIH-VRIGDFGLAcpdilQDGNDSTTMSRLNGLTHTSGVGTCLYAAPE 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 224 THLGKEQSRRDDLEALGHMFMYFLRgslPWqglkaDTLKERYQKIGDTKRATPIEVLCENFPEelatYLRYVRRL 298
Cdd:cd14049  204 QLEGSHYDFKSDMYSIGVILLELFQ---PF-----GTEMERAEVLTQLRNGQIPKSLCKRWPV----QAKYIKLL 266
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
46-258 3.13e-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: 42.38  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ-------LHLEYRFYKQLgQSEGVPQvyYFGPCGKYNAL 118
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPEtskevsaLECEIQLLKNL-QHERIVQ--YYGCLRDRAEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 VLELL-----GPSLED-------LFDLCDRKFSLktvlmiaiQLVTRMEYVHSKHLIYRDVKPENFLigRQSAKKqhiIY 186
Cdd:cd06651   85 TLTIFmeympGGSVKDqlkaygaLTESVTRKYTR--------QILEGMSYLHSNMIVHRDIKGANIL--RDSAGN---VK 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 187 IIDFGLAKEYidpeTHKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 258
Cdd:cd06651  152 LGDFGASKRL----QTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEA 219
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
48-193 3.18e-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: 42.50  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  48 RVGKKIGCGNFGELRLGKNLYNNEHVAIKL----EPMKSRApqLHLEYRFYKQLGQSEGVPQVY---YFGP------CGK 114
Cdd:cd14036    3 RIKRVIAEGGFAFVYEAQDVGTGKEYALKRllsnEEEKNKA--IIQEINFMKKLSGHPNIVQFCsaaSIGKeesdqgQAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 115 YnALVLELLGPSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKH--LIYRDVKPENFLIGRQSakkqhIIYIIDF 190
Cdd:cd14036   81 Y-LLLTELCKGQLVDFVKKVEAPgpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQG-----QIKLCDF 154

                 ...
gi 919096895 191 GLA 193
Cdd:cd14036  155 GSA 157
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
149-276 3.20e-04

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: 42.23  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK--EYiDPEthkhipyrEHKSLTGTARYMSINTHL 226
Cdd:cd14187  115 QIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVK-----IGDFGLATkvEY-DGE--------RKKTLCGTPNYIAPEVLS 180
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 919096895 227 GKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATP 276
Cdd:cd14187  181 KKGHSFEVDIWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIP 227
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
52-194 3.23e-04

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 42.24  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRlgKNLYNNEH----VAIKL---EPMKSRAPQLHLEYRFYKQLGQSEGVPQVyyfGPCGKYN-ALVLELL 123
Cdd:cd05115   11 ELGSGNFGCVK--KGVYKMRKkqidVAIKVlkqGNEKAVRDEMMREAQIMHQLDNPYIVRMI---GVCEAEAlMLVMEMA 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 124 --GPsLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAK 194
Cdd:cd05115   86 sgGP-LNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL-----VNQHYAKISDFGLSK 152
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-207 3.70e-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: 42.18  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEP---MKSRAPQLHLEYRFYKQLGQSEGVP-QVYYFGPCGKYnaLVLEL 122
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPkkaLRGKEAMVENEIAVLRRINHENIVSlEDIYESPTHLY--LAMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LGPSleDLFD-LCDR-KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGR--QSAKkqhiIYIIDFGLAK---- 194
Cdd:cd14169   83 VTGG--ELFDrIIERgSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfEDSK----IMISDFGLSKieaq 156
                        170       180
                 ....*....|....*....|...
gi 919096895 195 ----------EYIDPETHKHIPY 207
Cdd:cd14169  157 gmlstacgtpGYVAPELLEQKPY 179
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
47-194 3.83e-04

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 42.13  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLG--KNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLgQSEGVPQVYYFGPCGKYNALVLELLg 124
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAvdSTTETDAHCAVKIFEVSDEASEAVREFESLRTL-QHENVQRLIAAFKPSNFAYLVMEKL- 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 125 psLEDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHIIYIIDFGLAK 194
Cdd:cd14112   83 --QEDVFTrfSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMF---QSVRSWQVKLVDFGRAQ 149
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
133-194 4.09e-04

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: 42.16  E-value: 4.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 133 LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhIIYIIDFGLAK 194
Cdd:cd13977  126 LLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGEP--ILKVADFGLSK 185
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
136-268 4.33e-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: 42.20  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsAKKQHiIYIIDFGLAKEYIdpethkhipyrEHKSLT- 214
Cdd:cd05570   91 RRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL----DAEGH-IKIADFGMCKEGI-----------WGGNTTs 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 215 ---GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd05570  155 tfcGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEG---DDEDELFEAI 208
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
136-271 4.48e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 42.55  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYIDPethkhIPYREHKSLTG 215
Cdd:PTZ00283 138 RTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG-----LVKLGDFGFSKMYAAT-----VSDDVGRTFCG 207
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 216 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-----TLKERYQKIGDT 271
Cdd:PTZ00283 208 TPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEevmhkTLAGRYDPLPPS 268
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
47-193 4.75e-04

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 42.38  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEY--RFYKQLGQSEGVPQVYYFGPCGKYNALVLE 121
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIlknHPSYARQGQIEVSIlaRLSTESADDYNFVRAYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919096895 122 LLGPSLEDLfdLCDRKFS---LKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSaKKQHIIYIIDFGLA 193
Cdd:cd14227   97 MLEQNLYDF--LKQNKFSplpLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPS-RQPYRVKVIDFGSA 168
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
149-199 5.90e-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: 41.89  E-value: 5.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQsAKKQHIIYIIDFGLAKEYIDP 199
Cdd:cd07842  116 QILNGIHYLHSNWVLHRDLKPANILVMGE-GPERGVVKIGDLGLARLFNAP 165
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
138-258 6.01e-04

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: 41.65  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 138 FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYIDPETHKHIpyrehksltGTA 217
Cdd:cd05606   95 FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHG----H-VRISDLGLACDFSKKKPHASV---------GTH 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 919096895 218 RYMSINTHL-GKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 258
Cdd:cd05606  161 GYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKT 202
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
149-195 6.93e-04

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: 41.20  E-value: 6.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPEN-FLIGRQSAKkqhiiyIIDFGLAKE 195
Cdd:cd14046  112 QILEGLAYIHSQGIIHRDLKPVNiFLDSNGNVK------IGDFGLATS 153
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
118-214 6.94e-04

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 41.67  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRkFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKEYI 197
Cdd:PTZ00024  97 LVMDIMASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFI-----NSKGICKIADFGLARRYG 170
                         90
                 ....*....|....*..
gi 919096895 198 DPETHKHIPYREHKSLT 214
Cdd:PTZ00024 171 YPPYSDTLSKDETMQRR 187
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
109-221 7.32e-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: 41.56  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 109 FGPCGKYNALVLELlgpsledlfdlcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYII 188
Cdd:cd06644   90 FCPGGAVDAIMLEL------------DRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD-----IKLA 152
                         90       100       110
                 ....*....|....*....|....*....|...
gi 919096895 189 DFGLAKEYIdpethKHIPYREhkSLTGTARYMS 221
Cdd:cd06644  153 DFGVSAKNV-----KTLQRRD--SFIGTPYWMA 178
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
118-219 8.18e-04

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: 41.33  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA---- 193
Cdd:cd07864   93 LVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIK-----LADFGLArlyn 167
                         90       100
                 ....*....|....*....|....*...
gi 919096895 194 KEYIDPETHKHIP--YREHKSLTGTARY 219
Cdd:cd07864  168 SEESRPYTNKVITlwYRPPELLLGEERY 195
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
49-319 8.55e-04

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer 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 Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 41.07  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFG---ELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEY-------------RFYKQLG-----QSEGVPQVY 107
Cdd:cd14204   11 LGKVLGEGEFGsvmEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFlseaacmkdfnhpNVIRLLGvclevGSQRIPKPM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 108 YFGPCGKYNALVLELLGPSLEDlfdlcDRKF-SLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIY 186
Cdd:cd14204   91 VILPFMKYGDLHSFLLRSRLGS-----GPQHvPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCML-----RDDMTVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 187 IIDFGLAKEYIDPEThkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLKErY 265
Cdd:cd14204  161 VADFGLSKKIYSGDY-----YRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGvTMWEIATRGMTPYPGVQNHEIYD-Y 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919096895 266 QKIGDtKRATPIEVLcenfpEELATYLRYVRRLDFFETPDYDYLRKLFTDLMAK 319
Cdd:cd14204  235 LLHGH-RLKQPEDCL-----DELYDIMYSCWRSDPTDRPTFTQLRENLEKLLES 282
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
149-196 9.45e-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: 41.24  E-value: 9.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEY 196
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNADCELK-----ICDFGLARGF 155
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-207 9.56e-04

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: 41.19  E-value: 9.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEP---MKSRAPQLHLEYRFYKQLGQSEGVP-QVYYFGPCGKYnaLVLEL 122
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPkkaLKGKESSIENEIAVLRKIKHENIVAlEDIYESPNHLY--LVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 123 LgpSLEDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKQhiIYIIDFGLAKE----- 195
Cdd:cd14168   90 V--SGGELFDRIVEKgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESK--IMISDFGLSKMegkgd 165
                        170       180
                 ....*....|....*....|..
gi 919096895 196 ----------YIDPETHKHIPY 207
Cdd:cd14168  166 vmstacgtpgYVAPEVLAQKPY 187
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
146-200 1.01e-03

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: 40.87  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLA--------------KEYIDPE 200
Cdd:cd14052  111 ILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLK-----IGDFGMAtvwplirgieregdREYIAPE 174
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
129-173 1.06e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 41.37  E-value: 1.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 129 DLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPEN-FL 173
Cdd:PHA03207 171 DLFTYVDRSgpLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENiFL 218
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
53-253 1.10e-03

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 40.81  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRLGKNLYNNEHVAIKLEPMK-----SRAPQLH----LEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELL 123
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKIHQLNkswrdEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHS--KHLIYRDVKPENFLIGRQSAKKQhiIYIIDFGLAKeYIDPET 201
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGE--IKITDFGLSK-IMDDDS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 202 HKHIPYREHKSLTGTARYMSINTH-LGKEQ---SRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd14040  171 YGVDGMDLTSQGAGTYWYLPPECFvVGKEPpkiSNKVDVWSVGVIFFQCLYGRKPF 226
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
138-221 1.11e-03

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: 40.80  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 138 FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYIDPEThkhipyreHKSLTGTA 217
Cdd:cd05605   99 FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHG----H-VRISDLGLAVEIPEGET--------IRGRVGTV 165

                 ....
gi 919096895 218 RYMS 221
Cdd:cd05605  166 GYMA 169
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
46-194 1.12e-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: 40.63  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKnlYNNEHVAIKLEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYnaLVLELLgp 125
Cdd:cd05083    7 KLTLGEIIGEGEFGAVLQGE--YMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLY--IVMELM-- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919096895 126 SLEDLFDLCDRK----FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd05083   81 SKGNLVNFLRSRgralVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAK-----ISDFGLAK 148
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
51-193 1.23e-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: 40.78  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  51 KKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQ-----LHLEYRFYKQLGQsegvPQVYYFGPC--GKYNA-LVLEL 122
Cdd:cd06634   21 REIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNekwqdIIKEVKFLQKLRH----PNTIEYRGCylREHTAwLVMEY 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 123 LGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLA 193
Cdd:cd06634   97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPG-----LVKLGDFGSA 162
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
137-268 1.28e-03

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: 40.63  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHKHipyrehkSLTGT 216
Cdd:cd05585   90 RFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH-----IALCDFGLCKLNMKDDDKTN-------TFCGT 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 217 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 268
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYD---ENTNEMYRKI 206
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
146-261 1.38e-03

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: 40.45  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVtrmeYVHSKHLIYRDVKPENFLIGRQSakkqHiIYIIDFGLAKEYIDPEthkhipyREHKSLTGTARYMSINTH 225
Cdd:cd05587  106 IAVGLF----FLHSKGIIYRDLKLDNVMLDAEG----H-IKIADFGMCKEGIFGG-------KTTRTFCGTPDYIAPEII 169
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 919096895 226 LGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05587  170 AYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDEL 205
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
154-195 1.49e-03

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: 40.36  E-value: 1.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 919096895 154 MEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd05589  114 LQFLHEHKIVYRDLKLDNLLLDTEGYVK-----IADFGLCKE 150
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
118-262 1.52e-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: 40.26  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLgpSLEDLFDLC---DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQHIIYIIDFGLAK 194
Cdd:cd14114   76 LILEFL--SGGELFERIaaeHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMC---TTKRSNEVKLIDFGLAT 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 195 EyIDPEthkhipyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-TLK 262
Cdd:cd14114  151 H-LDPK-------ESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDeTLR 211
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
118-193 1.52e-03

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: 40.36  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919096895 118 LVLELLGPSleDLFD--LCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI-GRQSAKKQhiIYIIDFGLA 193
Cdd:cd14183   81 LVMELVKGG--DLFDaiTSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKS--LKLGDFGLA 155
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
149-196 1.56e-03

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: 40.33  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEY 196
Cdd:cd07863  116 QFLRGLDFLHANCIVHRDLKPENILVTSGGQVK-----LADFGLARIY 158
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
135-280 1.64e-03

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: 40.25  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHKHipyrehkSLT 214
Cdd:cd05586   90 EGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGH-----IALCDFGLSKADLTDNKTTN-------TFC 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919096895 215 GTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRGslpWQGLKADTLKERYQKIGDTKRATPIEVL 280
Cdd:cd05586  158 GTTEYLAPEVLLDeKGYTKMVDFWSLGVLVFEMCCG---WSPFYAEDTQQMYRNIAFGKVRFPKDVL 221
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
141-196 1.80e-03

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: 40.02  E-value: 1.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 141 KTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqSAKKQhiIYIIDFGLAKEY 196
Cdd:cd07862  110 ETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV---TSSGQ--IKLADFGLARIY 160
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-252 1.99e-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: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKH-LIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHkhipyrehkSLTGTARYMSINT 224
Cdd:cd06649  108 VSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMAN---------SFVGTRSYMSPER 173
                         90       100
                 ....*....|....*....|....*...
gi 919096895 225 HLGKEQSRRDDLEALGHMFMYFLRGSLP 252
Cdd:cd06649  174 LQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
148-240 2.10e-03

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 39.73  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 148 IQLVTRMEYVHSKHLIYRDVKPEN-FLigrqsaKKQHIIYIIDFGLAKEYidpETHKHIPyrehKSLTGTARYMSINTHL 226
Cdd:cd08223  109 VQIAMALQYMHERNILHRDLKTQNiFL------TKSNIIKVGDLGIARVL---ESSSDMA----TTLIGTPYYMSPELFS 175
                         90
                 ....*....|....
gi 919096895 227 GKEQSRRDDLEALG 240
Cdd:cd08223  176 NKPYNHKSDVWALG 189
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
136-197 2.39e-03

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: 39.89  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYI 197
Cdd:cd05590   91 RRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCK-----LADFGMCKEGI 147
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
126-293 2.40e-03

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 39.68  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 126 SLEDLfdLCDRKFSLKTVLMIAI--QLVTRMEYVHSKHLIYR-DVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPETH 202
Cdd:cd13992   82 SLQDV--LLNREIKMDWMFKSSFikDIVKGMNYLHSSSIGYHgRLKSSNCLVDSRWVVK-----LTDFGLRNLLEEQTNH 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 KHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY--FLRgSLPWQGLKADTLKERYQKIG-DTKRATPIEV 279
Cdd:cd13992  155 QLDEDAQHKKLLWTAPELLRGSLLEVRGTQKGDVYSFA-IILYeiLFR-SDPFALEREVAIVEKVISGGnKPFRPELAVL 232
                        170
                 ....*....|....
gi 919096895 280 LCEnFPEELATYLR 293
Cdd:cd13992  233 LDE-FPPRLVLLVK 245
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
46-193 2.59e-03

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 40.07  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRAPQLHLEY--RFYKQLGQSEGVPQVYYFGPCGKYNALVL 120
Cdd:cd14228   16 SYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIlknHPSYARQGQIEVSIlsRLSSENADEYNFVRSYECFQHKNHTCLVF 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 121 ELLGPSLEDLfdLCDRKFS---LKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgRQSAKKQHIIYIIDFGLA 193
Cdd:cd14228   96 EMLEQNLYDF--LKQNKFSplpLKYIRPILQQVATALMKLKSLGLIHADLKPENIML-VDPVRQPYRVKVIDFGSA 168
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
47-258 2.74e-03

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: 39.71  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEH----VAIKlEPMKSRAPQLHLEY-RFYKQLGQSEGVPQVYYFGPC-GKYNALVL 120
Cdd:cd05057    9 LEKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIK-VLREETGPKANEEIlDEAYVMASVDHPHLVRLLGIClSSQVQLIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 121 EL--LGPSLEDLFDLCDRKFSlKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLAKeYID 198
Cdd:cd05057   88 QLmpLGCLLDYVRNHRDNIGS-QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV-----KTPNHVKITDFGLAK-LLD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 199 PEtHKHIPYREHKSltgTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKA 258
Cdd:cd05057  161 VD-EKEYHAEGGKV---PIKWMALESIQYRIYTHKSDVWSYGvTVWELMTFGAKPYEGIPA 217
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
47-195 2.78e-03

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 39.61  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQSEGVPQvyYFG------PCGKYNAL- 118
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKvMDVTEDEEEEIKLEINMLKKYSHHRNIAT--YYGafikksPPGHDDQLw 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 119 -VLELLGP-SLEDLF-DLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd06636   96 lVMEFCGAgSVTDLVkNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVK-----LVDFGVSAQ 170
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
49-255 2.83e-03

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 39.71  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  49 VGKKIGCGNFGELRLGKNLYNNEHVAIKL---EPMKSRApQLHLEYRFYKQLGQSEGVPQ-VYYFGPCGKYnALVLELL- 123
Cdd:cd14090    6 TGELLGEGAYASVQTCINLYTGKEYAVKIiekHPGHSRS-RVFREVETLHQCQGHPNILQlIEYFEDDERF-YLVFEKMr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDlcDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAK------EY 196
Cdd:cd14090   84 gGPLLSHIEK--RVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILC--ESMDKVSPVKICDFDLGSgiklssTS 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919096895 197 IDPEThkhIPyrEHKSLTGTARYMS---INTHLGKEQS--RRDDLEALGHMFMYFLRGSLPWQG 255
Cdd:cd14090  160 MTPVT---TP--ELLTPVGSAEYMApevVDAFVGEALSydKRCDLWSLGVILYIMLCGYPPFYG 218
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
136-212 2.94e-03

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 39.33  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPEN-FLigrqsakKQHIIYIIDFGLAK----------------EYID 198
Cdd:cd08222  101 TTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNiFL-------KNNVIKVGDFGISRilmgtsdlattftgtpYYMS 173
                         90
                 ....*....|....
gi 919096895 199 PETHKHIPYrEHKS 212
Cdd:cd08222  174 PEVLKHEGY-NSKS 186
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
114-201 2.96e-03

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: 39.41  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 114 KYNALVLELLGPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrqsaKKQHIIYIIDFGLA 193
Cdd:cd14154   64 KLNLITEYIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLV-----REDKTVVVADFGLA 138

                 ....*...
gi 919096895 194 KEYIDPET 201
Cdd:cd14154  139 RLIVEERL 146
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
117-194 3.72e-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: 38.87  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 117 ALVLELLGPSleDLFDLCDRK--FSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkQHIIYIIDFGLAK 194
Cdd:cd14106   84 ILILELAAGG--ELQTLLDEEecLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFP--LGDIKLCDFGISR 159
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
136-174 3.72e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 39.49  E-value: 3.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLI 174
Cdd:PHA03211 255 RPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLV 293
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
53-194 3.81e-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: 39.11  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  53 IGCGNFGELRL------GKNlyNNEHVAIKlEPMKSRAPQL---HLEYRFYKQLgQSEGVpqVYYFGPCgkYNA------ 117
Cdd:cd05081   12 LGKGNFGSVELcrydplGDN--TGALVAVK-QLQHSGPDQQrdfQREIQILKAL-HSDFI--VKYRGVS--YGPgrrslr 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919096895 118 LVLELL-GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAK 194
Cdd:cd05081   84 LVMEYLpSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVK-----IADFGLAK 156
PRK14879 PRK14879
Kae1-associated kinase Bud32;
103-268 4.07e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 38.35  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 103 VPQVYYFGPcGKYnALVLELL-GPSLEDLFDLCDRKFsLKTVLMIAIQlVTRMeyvHSKHLIYRDVKPENFLI-GRQsak 180
Cdd:PRK14879  63 VPAVYFVDP-ENF-IIVMEYIeGEPLKDLINSNGMEE-LELSREIGRL-VGKL---HSAGIIHGDLTTSNMILsGGK--- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 181 kqhiIYIIDFGLAKEYIDPETHK---HIPYREHKSLTGtarymsinthlgkeqsrrddlEALGHMFMYFLRGSLPWQGLK 257
Cdd:PRK14879 133 ----IYLIDFGLAEFSKDLEDRAvdlHVLLRSLESTHP---------------------DWAEELFEAFLEGYREVMGEK 187
                        170
                 ....*....|.
gi 919096895 258 ADTLKERYQKI 268
Cdd:PRK14879 188 AEEVLERVKEI 198
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
92-253 4.65e-03

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 38.84  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  92 RFYKQLGQSEGVPQVYYFGPCGKYNALvLELLGPSLEDLFDLCDRK----FSLKTVLMIAIQLVTRMEYVHSKHLIYRDV 167
Cdd:cd05094   71 KFYGVCGDGDPLIMVFEYMKHGDLNKF-LRAHGPDAMILVDGQPRQakgeLGLSQMLHIATQIASGMVYLASQHFVHRDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 168 KPENFLIGrqsakKQHIIYIIDFGLAKEYIDPEThkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGH-MFMYF 246
Cdd:cd05094  150 ATRNCLVG-----ANLLVKIGDFGMSRDVYSTDY-----YRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGViLWEIF 219

                 ....*..
gi 919096895 247 LRGSLPW 253
Cdd:cd05094  220 TYGKQPW 226
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
144-195 4.75e-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: 4.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 144 LMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKE 195
Cdd:cd05090  127 LHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVK-----ISDLGLSRE 173
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
137-261 4.85e-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: 38.82  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 137 KFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIdpethkhIPYREHKSLTGT 216
Cdd:cd05615  107 KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH-----IKIADFGMCKEHM-------VEGVTTRTFCGT 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 919096895 217 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 261
Cdd:cd05615  175 PDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDEL 219
PTZ00284 PTZ00284
protein kinase; Provisional
47-206 4.91e-03

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 39.18  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLE---PMKSRAPQLhlEYRFYKQLGQSEGVPQV------YYFGPCGKYNA 117
Cdd:PTZ00284 131 FKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVrnvPKYTRDAKI--EIQFMEKVRQADPADRFplmkiqRYFQNETGHMC 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 118 LVLELLGPSLEDLFdLCDRKFSLKTVLMIAIQLVTRMEYVHSK-HLIYRDVKPENFLIGRQSAKkqhiiyiidfglakey 196
Cdd:PTZ00284 209 IVMPKYGPCLLDWI-MKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDTV---------------- 271
                        170
                 ....*....|
gi 919096895 197 IDPETHKHIP 206
Cdd:PTZ00284 272 VDPVTNRALP 281
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
146-277 5.34e-03

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: 38.53  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKeyidpETHKHIPYREhkslTGTARYMSINTH 225
Cdd:cd08530  108 IFIQMLRGLKALHDQKILHRDLKSANILLSAGD-----LVKIGDLGISK-----VLKKNLAKTQ----IGTPLYAAPEVW 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919096895 226 LGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKrATPI 277
Cdd:cd08530  174 KGRPYDYKSDIWSLGCLLYEMATFRPPFE---ARTMQELRYKVCRGK-FPPI 221
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
140-193 5.46e-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: 38.57  E-value: 5.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919096895 140 LKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKkqhiIYIIDFGLA 193
Cdd:cd14013  119 NVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ----FKIIDLGAA 168
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
149-240 5.46e-03

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: 38.82  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSakkqhIIYIIDFGLAKEYIDPETHKHIPYrehkslTGTARYMSINTHLGK 228
Cdd:cd07848  108 QLIKAIHWCHKNDIVHRDIKPENLLISHND-----VLKLCDFGFARNLSEGSNANYTEY------VATRWYRSPELLLGA 176
                         90
                 ....*....|..
gi 919096895 229 EQSRRDDLEALG 240
Cdd:cd07848  177 PYGKAVDMWSVG 188
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
135-195 5.60e-03

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: 38.42  E-value: 5.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919096895 135 DRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIgrQSAKKQHIIYIIDFGLAKE 195
Cdd:cd14089   94 DSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLY--SSKGPNAILKLTDFGFAKE 152
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
149-204 6.01e-03

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: 38.82  E-value: 6.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919096895 149 QLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKeYIDPEtHKH 204
Cdd:cd07849  114 QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLK-----ICDFGLAR-IADPE-HDH 162
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-240 6.25e-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: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 146 IAIQLVTRMEYVHSKH-LIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHkhipyrehkSLTGTARYMSINT 224
Cdd:cd06615  104 ISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMAN---------SFVGTRSYMSPER 169
                         90
                 ....*....|....*.
gi 919096895 225 HLGKEQSRRDDLEALG 240
Cdd:cd06615  170 LQGTHYTVQSDIWSLG 185
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
46-315 6.26e-03

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 38.51  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  46 NFRVGKKIGCGNFGELRLGkNLYNNEHVAIKLEPMKSRAPQLHL-EYRFYKQLgQSEGVPQVYYFgPCGKYNALVLELL- 123
Cdd:cd05071   10 SLRLEVKLGQGCFGEVWMG-TWNGTTRVAIKTLKPGTMSPEAFLqEAQVMKKL-RHEKLVQLYAV-VSEEPIYIVTEYMs 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 124 -GPSLEDLFDLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEYIDPEth 202
Cdd:cd05071   87 kGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCK-----VADFGLARLIEDNE-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 203 khipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYF-LRGSLPWQGLKADTLKERYQKigDTKRATPIEVlc 281
Cdd:cd05071  160 ----YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELtTKGRVPYPGMVNREVLDQVER--GYRMPCPPEC-- 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 919096895 282 enfPEELATYLRYVRRLDFFETPDYDYLRKLFTD 315
Cdd:cd05071  232 ---PESLHDLMCQCWRKEPEERPTFEYLQAFLED 262
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
92-208 6.63e-03

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 38.22  E-value: 6.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  92 RFYKQLGQSEGVPQVYYFGPCGKYNALvLELLGPSLEDLF--DLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKP 169
Cdd:cd05049   72 KFYGVCTEGDPLLMVFEYMEHGDLNKF-LRSHGPDAAFLAseDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLAT 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919096895 170 ENFLIGRQSAKKqhiiyIIDFGLAK-----EYIDPETHKHIPYR 208
Cdd:cd05049  151 RNCLVGTNLVVK-----IGDFGMSRdiystDYYRVGGHTMLPIR 189
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
156-200 6.81e-03

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: 38.28  E-value: 6.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 919096895 156 YVHSKHLIYRDVKPENFLIGRQSAKKqhiiyIIDFGLAKEyIDPE 200
Cdd:cd07834  118 YLHSAGVIHRDLKPSNILVNSNCDLK-----ICDFGLARG-VDPD 156
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
52-253 7.02e-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: 38.48  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895  52 KIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAPQLHLEYRFYKQLGQSEGVPQVYYFGPCGKYNALVLELL-GPSLED 129
Cdd:cd06658   29 KIGEGSTGIVCIATEKHTGKQVAVKkMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLeGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 130 LfdLCDRKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKeyidpETHKHIPYRe 209
Cdd:cd06658  109 I--VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR-----IKLSDFGFCA-----QVSKEVPKR- 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 919096895 210 hKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd06658  176 -KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY 218
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
136-253 7.23e-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: 38.46  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919096895 136 RKFSLKTVLMIAIQLVTRMEYVHSKHLIYRDVKPENFLIGRQSAkkqhiIYIIDFGLAKEYIDPETHKhipyrehKSLTG 215
Cdd:cd05617  111 RKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH-----IKLTDYGMCKEGLGPGDTT-------STFCG 178
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919096895 216 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 253
Cdd:cd05617  179 TPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
Pkinase pfam00069
Protein kinase domain;
47-76 8.54e-03

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 37.61  E-value: 8.54e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 919096895   47 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK 76
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK 30
 
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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