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Conserved domains on  [gi|116812624|ref|NP_775771|]
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tau-tubulin kinase 2 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
27-219 4.07e-36

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 137.75  E-value: 4.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQL-QGRNLA 102
Cdd:cd00180     1 LGEGGFGTVYLARDKKTGKKVAIKIikkEDSSSLLEELLREIEILKKLNHP-NIVKLYGVFEDENHLYLVMEYcEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  103 DLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFTNSCGDVRPpra 182
Cdd:cd00180    80 DLLKEN-EGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLD---SDNGKVKLADFGLSKLLTSDKSLLKT--- 152
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 116812624  183 vagFRGTVRYASINAHRNR-EMGRHDDLWSLFYMLVEF 219
Cdd:cd00180   153 ---IVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYEL 187
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
27-219 4.07e-36

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 137.75  E-value: 4.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQL-QGRNLA 102
Cdd:cd00180     1 LGEGGFGTVYLARDKKTGKKVAIKIikkEDSSSLLEELLREIEILKKLNHP-NIVKLYGVFEDENHLYLVMEYcEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  103 DLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFTNSCGDVRPpra 182
Cdd:cd00180    80 DLLKEN-EGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLD---SDNGKVKLADFGLSKLLTSDKSLLKT--- 152
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 116812624  183 vagFRGTVRYASINAHRNR-EMGRHDDLWSLFYMLVEF 219
Cdd:cd00180   153 ---IVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYEL 187
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
19-281 4.07e-20

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 91.94  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYD---ALDMLTRENVALKVESAQQPKQVL----------KMEVAVLKKLQGKDH--VCRFIGC 83
Cdd:PHA02882   12 KEWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKIENLENETIVMetlvynniydIDKIALWKNIHNIDHlgIPKYYGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   84 G--RNDRFNYVVMQLQGRNLAD---LRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRK 158
Cdd:PHA02882   92 GsfKRCRMYYRFILLEKLVENTkeiFKRIKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMV----DGNNR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  159 CYMLDFGLARQFTNSCGDVRPPRAVAGF-RGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV-- 235
Cdd:PHA02882  165 GYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLih 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 116812624  236 ----GSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 281
Cdd:PHA02882  245 aakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIFD 294
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
87-173 2.34e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 39.51  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624    87 DRFNYV-VMQ-LQGRNLADLRRSqsrgtftisTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgRFPStcRKCYMLDF 164
Cdd:TIGR03724   68 DPDNKTiVMEyIEGKPLKDVIEE---------GNDELLREIGRLVGKLHKAGIVHGDLTTSNI---IVRD--DKLYLIDF 133

                   ....*....
gi 116812624   165 GLARqFTNS 173
Cdd:TIGR03724  134 GLGK-YSDE 141
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
93-168 2.77e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 39.50  E-value: 2.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116812624   93 VMQ-LQGRNLADLRRSQSRGTFTISttLRLGRQIlesiESIHSVGFLHRDIKPSNFAMgrfpsTCRKCYMLDFGLAR 168
Cdd:PRK14879   77 VMEyIEGEPLKDLINSNGMEELELS--REIGRLV----GKLHSAGIIHGDLTTSNMIL-----SGGKIYLIDFGLAE 142
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
87-173 9.40e-03

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 37.65  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   87 DRFNY-VVMQ-LQGRNLADlrrsqsrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpstcRKCYMLDF 164
Cdd:COG3642    70 DPDNGlIVMEyIEGELLKD---------ALEEARPDLLREVGRLVGKLHKAGIVHGDLTTSNIILSG-----GRIYFIDF 135

                  ....*....
gi 116812624  165 GLARqFTNS 173
Cdd:COG3642   136 GLGE-FSDE 143
Pkinase pfam00069
Protein kinase domain;
21-256 4.00e-34

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 133.14  E-value: 4.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624    21 WKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPK----QVLKMEVAVLKKLQGkDHVCRFIGCGRNDRFNYVVMQL 96
Cdd:pfam00069    1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKskkdQTARREIRILRRLSH-PNIVRLIDAFEDKDHLYLVMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624    97 -QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCrkcyMLDFGLARQFTNSCG 175
Cdd:pfam00069   80 cEGGDLFDYLSR--GGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVK----IADFGLAKKLTKSSS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   176 DVRppravaGFRGTVRYASINAHRNREM-GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQvgsiKERYDHRLMLKHLPPE 254
Cdd:pfam00069  154 SLT------TFVGTPEYMAPEVLLGGNGyGPKVDVWSLGVILYELLTGKPPFSGESILDQ----LQLIRRILGPPLEFDE 223

                   ..
gi 116812624   255 FS 256
Cdd:pfam00069  224 PK 225
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
21-264 2.04e-30

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 122.25  E-value: 2.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624     21 WKVLRKIGGGGFGEIYDALDMLTRENVALKV----ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNDRFNYVVMQL 96
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVikkkKIKKDRERILR-EIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624     97 -QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTnscg 175
Cdd:smart00220   79 cEGGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL----DEDGHVKLADFGLARQLD---- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624    176 dvrPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRkikDKEQVGSIKERydhrlmLKHLPPEF 255
Cdd:smart00220  149 ---PGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP---GDDQLLELFKK------IGKPKPPF 216

                    ....*....
gi 116812624    256 SIFLDHISS 264
Cdd:smart00220  217 PPPEWDISP 225
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
21-261 1.86e-29

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 122.16  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDmltRENVALKV-----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQ 95
Cdd:COG0515     2 YRILRKLGEGSFGEVYLARD---RKLVALKVlakklESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   96 -LQGRNLADL-RRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcRKCYMLDFGLARQFTNS 173
Cdd:COG0515    79 yVDGGSLEDLlKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDG---RVVKLIDFGLAKLLPDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  174 CGDVRPPRAVAGFRGTVRYASINAHR---NREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK---EQVGSIKERYDHRLM 247
Cdd:COG0515   156 GSTSSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSsatSQTLKIILELPTPSL 235
                         250
                  ....*....|....
gi 116812624  248 LKHLPPEFSIFLDH 261
Cdd:COG0515   236 ASPLSPSNPELISK 249
pknD PRK13184
serine/threonine-protein kinase; Reviewed
19-256 1.84e-11

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 67.49  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDMLTRENVALK------VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNDRFNYV 92
Cdd:PRK13184    2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKkiredlSENPLLKKRFLR-EAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   93 VMQLQGRNLADLRRS----------QSRGTfTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcrKCYML 162
Cdd:PRK13184   81 MPYIEGYTLKSLLKSvwqkeslskeLAEKT-SVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVVIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  163 DFGLAR--------------QFTNSCGD--VRPPRAVagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:PRK13184  156 DWGAAIfkkleeedlldidvDERNICYSsmTIPGKIV----GTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 116812624  227 R-----KIKDKEQVGSIKERYDHRlmlkHLPPEFS 256
Cdd:PRK13184  232 RrkkgrKISYRDVILSPIEVAPYR----EIPPFLS 262
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
19-170 4.40e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 60.99  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQ-----PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNDRFNYVV 93
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQedegvPSTAIR-EISLLKEMQ-HGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   94 MQLQGRNLadlrRSQSRGTFTISTTLRLGR----QILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGLARQ 169
Cdd:PLN00009   80 FEYLDLDL----KKHMDSSPDFAKNPRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALK---LADFGLARA 152

                  .
gi 116812624  170 F 170
Cdd:PLN00009  153 F 153
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
21-222 5.63e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 58.51  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALKvESAQQPkQVLKMEVAVLKKLQG------KDHVcrFIGCGRNDRFNY--- 91
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIK-KVLQDP-QYKNRELLIMKNLNHiniiflKDYY--YTECFKKNEKNIfln 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   92 VVMQLQGRNLADLRRSQSRGTFTISTTL-RL-GRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCymlDFGLARQ 169
Cdd:PTZ00036  144 VVMEFIPQTVHKYMKHYARNNHALPLFLvKLySYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLC---DFGSAKN 220
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  170 FtnscgdvrppraVAGFRgTVRYASINAHRNREM-------GRHDDLWSLFYMLVEFVVG 222
Cdd:PTZ00036  221 L------------LAGQR-SVSYICSRFYRAPELmlgatnyTTHIDLWSLGCIIAEMILG 267
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
43-166 6.11e-05

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 45.99  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624    43 TRENVALKV------ESAQQPKQvLKMEVAVLKKLQgKDHVCRFIGCGR-NDRFNYVVMQL-QGRNLADlrRSQSRGTFT 114
Cdd:TIGR03903    2 TGHEVAIKLlrtdapEEEHQRAR-FRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYvPGRTLRE--VLAADGALP 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 116812624   115 ISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKCYM-LDFGL 166
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQ--TGVRPHAKvLDFGI 128
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
108-285 1.21e-03

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 41.00  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  108 QSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcRKCYMLDFGLARQF-TNSCGDvrppravagf 186
Cdd:PHA03390  101 KKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAK---DRIYLCDYGLCKIIgTPSCYD---------- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  187 rGTVRYAS---INAHRNremGRHDDLWSLFYMLVEFVVGQLPWRKIKDKE-QVGSIKERYDHRL-MLKHLPPEFSIFLDH 261
Cdd:PHA03390  168 -GTLDYFSpekIKGHNY---DVSFDWWAVGVLTYELLTGKHPFKEDEDEElDLESLLKRQQKKLpFIKNVSKNANDFVQS 243
                         170       180
                  ....*....|....*....|....
gi 116812624  262 ISSLDYftkpDYQLltSVFDNSIK 285
Cdd:PHA03390  244 MLKYNI----NYRL--TNYNEIIK 261
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
27-219 4.07e-36

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 137.75  E-value: 4.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQL-QGRNLA 102
Cdd:cd00180     1 LGEGGFGTVYLARDKKTGKKVAIKIikkEDSSSLLEELLREIEILKKLNHP-NIVKLYGVFEDENHLYLVMEYcEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  103 DLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFTNSCGDVRPpra 182
Cdd:cd00180    80 DLLKEN-EGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLD---SDNGKVKLADFGLSKLLTSDKSLLKT--- 152
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 116812624  183 vagFRGTVRYASINAHRNR-EMGRHDDLWSLFYMLVEF 219
Cdd:cd00180   153 ---IVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYEL 187
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
20-261 8.88e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 108.80  E-value: 8.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFN--YVV 93
Cdd:cd06606     1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSvelsGDSEEELEALEREIRILSSLQHP-NIVRYYGSERDEEKNtlNIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   94 MQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN---FAMGRfpstcrkCYMLDFGLARQ 169
Cdd:cd06606    80 LEYvSGGSLSSLLKK--FGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANilvDSDGV-------VKLADFGCAKR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  170 FtnscGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV----GSIKErydHR 245
Cdd:cd06606   151 L----GDIETGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSELGNPMAAlykiGSSGE---PP 223
                         250
                  ....*....|....*.
gi 116812624  246 LMLKHLPPEFSIFLDH 261
Cdd:cd06606   224 EIPEHLSEEAKDFLRK 239
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
19-281 4.07e-20

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 91.94  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYD---ALDMLTRENVALKVESAQQPKQVL----------KMEVAVLKKLQGKDH--VCRFIGC 83
Cdd:PHA02882   12 KEWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKIENLENETIVMetlvynniydIDKIALWKNIHNIDHlgIPKYYGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   84 G--RNDRFNYVVMQLQGRNLAD---LRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRK 158
Cdd:PHA02882   92 GsfKRCRMYYRFILLEKLVENTkeiFKRIKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMV----DGNNR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  159 CYMLDFGLARQFTNSCGDVRPPRAVAGF-RGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV-- 235
Cdd:PHA02882  165 GYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLih 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 116812624  236 ----GSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 281
Cdd:PHA02882  245 aakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIFD 294
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
21-228 6.42e-20

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 90.73  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKmEVAVLKKLQGKDHVcRFIGCGRNDRFNYVVM-QL 96
Cdd:cd05122     2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKViklESKEKKEKIIN-EIQILKKCKHPNIV-KYYGSYLKKDELWIVMeFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   97 QGRNLADLRRSqSRGTFT---ISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNS 173
Cdd:cd05122    80 SGGSLKDLLKS-TNQTLTesqIAYVC---KELLKGLEYLHSNGIIHRDIKAANILL----TSDGEVKLIDFGLSAQLSDT 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116812624  174 CGDVRppravagFRGTVRYAS---INAhrnremGRHD---DLWSLFYMLVEFVVGQLPWRK 228
Cdd:cd05122   152 KARNT-------MVGTPYWMApevING------KPYDykaDIWSLGITAIELAEGKPPYSE 199
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
20-226 7.63e-18

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 84.70  E-value: 7.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPKQVL----KMEVAVLKKLqgkDH--VCRFIGCGRNDRFNYVV 93
Cdd:cd06626     1 RWQRGNKIGGGTFGKVYTAVNLDTGELMAVKEIRIQDNDPKTikeiADEMKVLELL---KHpnLVKYYGVEVHREKVYIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   94 MQL-QGRNLADLrrsqsrgtftisttLRLGR------------QILESIESIHSVGFLHRDIKPSNFAMGrfpstcrKCY 160
Cdd:cd06626    78 MEYcSGGTLEEL--------------LEHGRildehvirvytlQLLEGLAYLHSHGIVHRDIKPANIFLD-------HNG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116812624  161 ML---DFGLARQFTNScgDVRPPRAVAGFRGTVRYAS---INAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06626   137 VIklgDFGCAVKLKNN--TTTMGEEVQSLAGTPAYMApevITGGKGKGHGRAADIWSLGCVVLEMATGKRPW 206
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine ...
20-172 2.20e-16

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173736 [Multi-domain]  Cd Length: 286  Bit Score: 80.02  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQ-----PKQVLKmEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVM 94
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRRleggiPNQALR-EIKALQACQHP-YVVKLLDVFPHGSGFVLVM 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116812624   95 QLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKcyMLDFGLARQFTN 172
Cdd:cd07832    79 EYMPSDLSEVLRDEER-PLPEAQVKSYMRMLLKGVAYMHANGIMHRDLKPANLLIS--ADGVLK--IADFGLARLFSE 151
STKc_MEKK3_like cd06625
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
21-226 1.01e-15

Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3-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. This subfamily is composed of MEKK3, MEKK2, and related proteins, all containing an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks), proteins that 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. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132956 [Multi-domain]  Cd Length: 263  Bit Score: 77.93  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRNDRFNYVV 93
Cdd:cd06625     4 WRRGKLLGQGAFGRVYLCYDVDTGRELAVKQvpfdpDSPETKKEVnaLECEIQLLKNLQ-HERIVQYYGCLRDDETLSIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   94 MQ-LQGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTN 172
Cdd:cd06625    83 MEyMPGGSVKDQLKAY--GALTETVTRKYTRQILEGVEYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRLQT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116812624  173 SCGDVRPPRAVAgfrGTVRYAS---INAHrnrEMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06625   157 ICSSGTGMKSVT---GTPYWMSpevISGE---GYGRKADVWSVGCTVVEMLTEKPPW 207
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
18-171 1.36e-15

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, 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 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.


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 77.64  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   18 KERWKVLRKIGGGGFGEIYDALDMLTRENVALKVES-AQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNDRFNYVVMQ- 95
Cdd:cd06614    18 RELYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRlRKQNKELIINEILIMKDCK-HPNIVDYYDSYLVGDELWVVMEy 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116812624   96 LQGRNLADLRRsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPStcrkCYMLDFGLARQFT 171
Cdd:cd06614    97 MDGGSLTDIIT-QNFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS----VKLADFGFAAQLT 167
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
20-259 2.35e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that 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. 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.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 76.69  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKV-------ESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNDRFNYV 92
Cdd:cd06632     1 RWRKGELLGSGSFGSVYEGLNLDDGDFFAVKEvsladdgQTGQEAVKQLEQEIALLSKLQHPNIV-QYLGTEREEDNLYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   93 VMQL-QGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKcyMLDFGLARQft 171
Cdd:cd06632    80 FLELvPGGSLAKLL--KKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGANILVD--TNGVVK--LADFGMAKQ-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  172 nscgdVRPPRAVAGFRGTVRY------ASINAHrnremGRHDDLWSLFYMLVEFVVGQLPWrkiKDKEQVGS---IKERY 242
Cdd:cd06632   152 -----VVEFSFAKSFKGSPYWmapeviAQQGGY-----GLAADIWSLGCTVLEMATGKPPW---SQLEGVAAvfkIGRSK 218
                         250
                  ....*....|....*..
gi 116812624  243 DHRLMLKHLPPEFSIFL 259
Cdd:cd06632   219 ELPPIPDHLSDEAKDFI 235
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
22-227 3.46e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 76.46  E-value: 3.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   22 KVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQ------PKQVlKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQ 95
Cdd:cd05581     4 KFGKIIGEGSFSTVVLAKEKETNKEYAIKILDKRQlikekkVKYV-KIEKEVLTRLNGHPGIIKLYYTFQDEENLYFVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   96 L-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCrkcyMLDFGLARQFTN-- 172
Cdd:cd05581    83 YaPNGELLQYIRK--YGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDKDMHIK----ITDFGTAKVLDPns 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116812624  173 --------SCGDVRPPRAV----AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 227
Cdd:cd05581   157 spesnkgdATNIDSQIEKNrrrfASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR 223
STKc_MEKK3_like_1 cd06653
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
19-226 5.10e-15

Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3)-like subfamily, catalytic (c) domain, functionally uncharacterized subgroup 1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3-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. The MEKK3-like subfamily is composed of MEKK3, MEKK2, and related proteins, all containing an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks), proteins that 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. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132984 [Multi-domain]  Cd Length: 264  Bit Score: 75.83  E-value: 5.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN---DR 88
Cdd:cd06653     2 VNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQvpfdpDSQETSKEVnaLECEIQLLKNLR-HDRIVQYYGCLRDpeeKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   89 FNYVVMQLQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLAR 168
Cdd:cd06653    81 LSIFVEYMPGGSIKD--QLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASK 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 116812624  169 QFTNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06653   155 RIQTICMSGTGIKSVT---GTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ...
21-170 7.74e-15

Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC 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. 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 similar proteins. 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.


Pssm-ID: 143333 [Multi-domain]  Cd Length: 283  Bit Score: 75.06  E-value: 7.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNDRFnYVVMQ 95
Cdd:cd05118     1 YQKLGKIGEGTYGVVYKARDKLTGEIVAIKkiklrFESEGIPKTALR-EIKLLKELNHPNIIKLLDVFRHKGDL-YLVFE 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116812624   96 LQGRNLADLRRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARQF 170
Cdd:cd05118    79 FMDTDLYKLIKDRQRG-LPESLIKSYLYQLLQGLAFCHSHGILHRDLKPENLLINT-EGVLKLA---DFGLARSF 148
STKc_p38beta_MAPK11 cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase; ...
17-223 7.79e-15

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), p38beta subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta. p38beta, also called 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.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 76.24  E-value: 7.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   17 VKERWKVLRKIGGGGFGEIYDALDMLTRENVALKVESaqQPKQVL------KMEVAVLKKLQGKDHVCR---FIGCGRND 87
Cdd:cd07878    13 VPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS--RPFQSLiharrtYRELRLLKHMKHENVIGLldvFTPATSIE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   88 RFN--YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDFG 165
Cdd:cd07878    91 NFNevYLVTNLMGADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNE---DC-ELRILDFG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116812624  166 LARQFTNScgdvrppraVAGFRGTVRYAS----IN-AHRNREMgrhdDLWSLFYMLVEFVVGQ 223
Cdd:cd07878   164 LARQADDE---------MTGYVATRWYRApeimLNwMHYNQTV----DIWSVGCIMAELLKGK 213
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine ...
22-180 8.38e-15

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Male germ cell-Associated Kinase (MAK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAK-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. 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 (ECO), 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.


Pssm-ID: 173734 [Multi-domain]  Cd Length: 283  Bit Score: 75.26  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   22 KVLRKIGGGGFGEIYDALDMLTRENVALKvesaqqpkqvlKM--------------EVAVLKKLQGKDHVCR----FIgc 83
Cdd:cd07830     2 KVIKQLGDGTFGSVYLARNKETGELVAIK-----------KMkkkfysweecmnlrEVKSLRKLNEHPNIVKlkevFR-- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   84 gRNDRFnYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfpsTCRKCYML- 162
Cdd:cd07830    69 -ENDEL-YFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENL-------LVSGPEVVk 139
                         170       180
                  ....*....|....*....|
gi 116812624  163 --DFGLARQFTNscgdvRPP 180
Cdd:cd07830   140 iaDFGLAREIRS-----RPP 154
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
26-185 9.77e-15

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 74.59  E-value: 9.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   26 KIGGGGFGEIYDALDMLTRENVALK-VESAQQPKQVLK---MEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQL-QGRN 100
Cdd:cd06627     7 LIGRGAFGVVYKGLNLETGDFVAIKqISLEKIKEEALKsimQEIDLLKNLKHP-NIVKYIGSIETSDSLYIILEYaENGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  101 LAD-LRRSqsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPStcrkCYMLDFGLArqfTNSCGDVRP 179
Cdd:cd06627    86 LRQiIKKF---GPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGV----VKLADFGVA---TKLNDVSKD 155

                  ....*.
gi 116812624  180 PRAVAG 185
Cdd:cd06627   156 DASVVG 161
STKc_MEKK2 cd06652
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 2; Serine ...
21-262 1.11e-14

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 2; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 2 (MEKK2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK2 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132983 [Multi-domain]  Cd Length: 265  Bit Score: 74.69  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--DRFNY 91
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQvqfdpESPETSKEVnaLECEIQLLKNLL-HERIVQYYGCLRDpmERTLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   92 VVMQLQ-GRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQF 170
Cdd:cd06652    83 IFMEHMpGGSIKD--QLKSYGALTENVTRKYTRQILEGVSYLHSNMIVHRDIKGANI----LRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  171 TNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYDHRLMLKH 250
Cdd:cd06652   157 QTICLSGTGMKSVT---GTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPVLPPH 233
                         250
                  ....*....|..
gi 116812624  251 LPPEFSIFLDHI 262
Cdd:cd06652   234 VSDHCRDFLKRI 245
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; Serine ...
15-169 1.58e-14

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), p38 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 75.02  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   15 ILVKERWKV------LRKIGGGGFGEIYDALDMLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---F 80
Cdd:cd07851     5 ELNKTVWEVpdryqnLSPVGSGAYGQVCSAFDTKTGRKVAIKklsrpFQSAIHAKRTYR-ELRLLKHMDHENVIGLldvF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   81 IGCGRNDRFN--YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrK 158
Cdd:cd07851    84 TPASSLEDFQdvYLVTHLMGADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNIAVN---EDC-E 156
                         170
                  ....*....|.
gi 116812624  159 CYMLDFGLARQ 169
Cdd:cd07851   157 LKILDFGLARH 167
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
19-173 3.55e-14

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. 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.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 73.03  E-value: 3.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQ 95
Cdd:cd06609     1 ELFTLLECIGKGSFGEVYKAIDKRTNQVVAIKVidlEEAEDEIEDIQQEIQFLSQCRSP-YITKYYGSFLKGSKLWIIME 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116812624   96 -LQGRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNS 173
Cdd:cd06609    80 yCGGGSCLDLLKPGKLDETYIAFIL---REVLLGLEYLHEEGKIHRDIKAANILL----SEEGDVKLADFGVSGQLTST 151
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine ...
24-171 4.71e-14

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


Pssm-ID: 173733 [Multi-domain]  Cd Length: 282  Bit Score: 72.90  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   24 LRKIGGGGFGEIYDALDMLTRENVALK-VESAQQ----PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNDRFNYVVMQLQG 98
Cdd:cd07829     4 LEKLGEGTYGVVYKARDKKTGEIVALKkIRLDNEeegiPSTALR-EISLLKELK-HPNIVKLLDVIHTERKLYLVFEYCD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116812624   99 RNLADLRRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLARQFT 171
Cdd:cd07829    82 MDLKKYLDKRPGP-LSPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNILINR--DGVLK--LADFGLARAFG 149
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine ...
21-226 5.78e-14

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 1 (MEKK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK1 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK1 activates the extracellular signal-regulated kinase 1/2 (ERK1/2) and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing.


Pssm-ID: 132961 [Multi-domain]  Cd Length: 268  Bit Score: 72.20  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDMLTRENVALKVESAQQPK--------QVLKMEVAVLKKLQgKDHVCRFIGCGRND-RFNY 91
Cdd:cd06630     2 WLKGQQLGTGAFSSCYQARDVKTGTLMAVKQVTYVRNTsseqeevvEALRKEIRLMARLN-HPHIIRMLGATCEDsHFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   92 VVMQLQGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFT 171
Cdd:cd06630    81 FVEWMAGGSVSHLLSKY--GAFKEAVIINYTEQLLRGLSYLHENQIIHRDVKGANLLID---STGQRLRIADFGAAARLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116812624  172 NSCgdVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06630   156 AKG--TGAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_ASK cd06624
Catalytic domain of the Protein Serine/Threonine Kinase, Apoptosis signal-regulating kinase; ...
27-226 6.52e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Apoptosis signal-regulating kinase; Serine/threonine kinases (STKs), Apoptosis signal-regulating kinase (ASK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Subfamily members are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) and include ASK1, ASK2, and MAPKKK15. 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. 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 (ROS)-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.


Pssm-ID: 173730 [Multi-domain]  Cd Length: 268  Bit Score: 72.17  E-value: 6.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALK--VESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGC-GRNDRFNYVVMQLQGRNLAD 103
Cdd:cd06624    16 LGKGTYGIVYAARDLSTQVRIAIKeiPERDSRYVQPLHEEIALHSYLKHRNIV-QYLGSdSENGFFKIFMEQVPGGSLSA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  104 LRRSQSRGTFTISTTLRL-GRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGLARQFT--NSCGDVrpp 180
Cdd:cd06624    95 LLRSKWGPLKDNEQTIIFyTKQILEGLKYLHDNQIVHRDIKGDNVLVNTYSGVVK---ISDFGTSKRLAgiNPCTET--- 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 116812624  181 ravagFRGTVRYAS--INAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06624   169 -----FTGTLQYMApeVIDKGPRGYGAPADIWSLGCTIVEMATGKPPF 211
STKc_MAPKKK_Byr2_like cd06628
Catalytic domain of fungal Byr2-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs) ...
27-280 1.00e-13

Catalytic domain of fungal Byr2-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, fungal Byr2-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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 (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. 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.


Pssm-ID: 173732 [Multi-domain]  Cd Length: 267  Bit Score: 71.80  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALK-VE----SAQQPKQ------VLKMEVAVLKKLQgKDHVCRFIGCGRN-DRFNYVVM 94
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKqVElpsvSASSKDRkrsmldALAREIALLKELQ-HENIVQYLGSSLDaDHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   95 QLQGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSC 174
Cdd:cd06628    87 YVPGGSVAALL--NNYGAFEETLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV----DNKGGIKISDFGISKKLEANS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  175 GDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKErydhrLMLKHLPPE 254
Cdd:cd06628   161 LSTKTNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGKHPFPDCTQLQAIFKIGE-----NASPEIPSN 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 116812624  255 FSI----FLDHISSLDYFTKPDY-QLLTSVF 280
Cdd:cd06628   236 ISSeaidFLEKTFEIDHNKRPTAaELLKHPF 266
STKc_p38gamma_MAPK12 cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase; ...
17-169 3.03e-13

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), p38gamma subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta. p38gamma, also called 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.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 71.14  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   17 VKERWKVLRKIGGGGFGEIYDALDMLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCGRNDR 88
Cdd:cd07880    13 VPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpFQSELFAKRAYR-ELRLLKHMKHENVIGLldvFTPDLSLDR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   89 FN--YVVMQLQGRNLADLRRSQSRGTFTISTtlrLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDFGL 166
Cdd:cd07880    92 FHdfYLVMPFMGTDLGKLMKHEKLSEDRIQF---LVYQMLKGLKYIHAAGIIHRDLKPGNLAVNE---DC-ELKILDFGL 164

                  ...
gi 116812624  167 ARQ 169
Cdd:cd07880   165 ARQ 167
STKc_MAPKKK_Bck1_like cd06629
Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs) ...
20-238 3.09e-13

Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, fungal Bck1-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. 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. 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.


Pssm-ID: 132960 [Multi-domain]  Cd Length: 272  Bit Score: 70.21  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALK-VE----SAQQPKQVLKMEVAVLKK----LQGKDH--VCRFIGCGR-ND 87
Cdd:cd06629     2 KWVKGELIGKGTYGRVYLALNVTTGEMMAVKqVElpatIAGRHDSRQKDMVKALRSeietLKDLDHlnIVQYLGFETtEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   88 RFNYVVMQLQGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRkcyMLDFGLA 167
Cdd:cd06629    82 YLSIFLEYVPGGSIGSCLRTY--GRFEEQLVRFFTEQVLEGLAYLHSKGILHRDLKADNLLVD-ADGICK---ISDFGIS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116812624  168 RQFTNSCGDVrpprAVAGFRGTVRYASINAHRNREMGRHD--DLWSLFYMLVEFVVGQLPWrkiKDKEQVGSI 238
Cdd:cd06629   156 KKSDDIYDND----QNMSMQGSVFWMAPEVIHSYSQGYSAkvDIWSLGCVVLEMFAGRRPW---SDEEAIAAM 221
STKc_MEKK3 cd06651
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 3; Serine ...
21-226 3.44e-13

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 3; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK3 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132982 [Multi-domain]  Cd Length: 266  Bit Score: 70.10  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDALDM-----LTRENVALKVESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--DRFNY 91
Cdd:cd06651     4 WRRGKLLGQGAFGRVYLCYDVdtgreLAAKQVQFDPESPETSKEVsaLECEIQLLKNLQ-HERIVQYYGCLRDraEKTLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   92 VVMQ-LQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQF 170
Cdd:cd06651    83 IFMEyMPGGSVKD--QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116812624  171 TNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06651   157 QTICMSGTGIRSVT---GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 209
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
27-225 4.03e-13

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 69.58  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALKVESAQQ-----PKQVLKMEVAVLKKLQGkDHVCRFIGCGRNDRFNYVVMQ-LQGRN 100
Cdd:cd05579     1 ISKGAYGRVFLAKKKSTGDIYAIKVIKKADmirknQVDQVLTERDILSQAQS-PYVVKLYYSFQGKKNLYLVMEyLPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  101 LADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcrkcymlDFGLARQ--FTNSCG 175
Cdd:cd05579    80 LASLLENV--GSLDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNIlidSNGHLKLT-------DFGLSKVglVRRQIN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 116812624  176 DVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 225
Cdd:cd05579   151 LNDDEKEDKRIVGTPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPP 200
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine ...
19-171 1.32e-12

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-dependent protein kinase like (CDKL) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 143338 [Multi-domain]  Cd Length: 288  Bit Score: 68.50  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDMLTRENVALK----VESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVM 94
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfkeSEDDEDVKKTALREVKVLRQLRHE-NIVNLKEAFRRKGRLYLVF 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116812624   95 QLQGRNLADLRRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARQFT 171
Cdd:cd07833    80 EYVERTLLELLEASPGG-LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSE-SGVLKLC---DFGFARALR 151
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
20-226 1.37e-12

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 68.06  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALK----VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFnYVVMQ 95
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKeidlTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRL-FIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   96 L-QGRNLADlRRSQSRGT-FTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYML-DFGLARQFTN 172
Cdd:cd08225    80 YcDGGDLMK-RINRQRGVlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI----FLSKNGMVAKLgDFGIARQLND 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116812624  173 ScgdVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd08225   155 S---MELAYTCV---GTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF 202
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
18-225 1.41e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 132972 [Multi-domain]  Cd Length: 277  Bit Score: 68.18  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   18 KERWKVLRKIGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVM 94
Cdd:cd06641     3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKDTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   95 Q-LQGRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTns 173
Cdd:cd06641    82 EyLGGGSALDLLEPGPLDETQIATIL---REILKGLDYLHSEKKIHRDIKAANVLL----SEHGEVKLADFGVAGQLT-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116812624  174 cgDVRPPRavAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 225
Cdd:cd06641   153 --DTQIKR--NTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
10-226 2.32e-12

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: 67.82  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   10 ILSVGIlVKERWKVLRKIGGGGFGEIYDALDMLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRND 87
Cdd:cd06656    11 IVSVGD-PKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKqMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   88 RFNYVVMQLQGRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLa 167
Cdd:cd06656    90 ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVC---RECLQALDFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF- 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  168 rqftnsCGDVRPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06656   162 ------CAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_MST4 cd06640
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; ...
18-225 3.75e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 4 (MST4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 67.00  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   18 KERWKVLRKIGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVM 94
Cdd:cd06640     3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKGTKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   95 Q-LQGRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTns 173
Cdd:cd06640    82 EyLGGGSALDLLRAGPFDEFQIATML---KEILKGLDYLHSEKKIHRDIKAANVLL----SEQGDVKLADFGVAGQLT-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116812624  174 cgDVRPPRAVagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 225
Cdd:cd06640   153 --DTQIKRNT--FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; Serine ...
20-169 5.38e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), Mitogen-Activated Protein Kinase (MAPK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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 main 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.


Pssm-ID: 173737 [Multi-domain]  Cd Length: 330  Bit Score: 67.17  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQPKQVLKmEVAVLKKLQGKD--HVCRFIGCGRNDRFN-- 90
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAVDKRTGRKVAIKKisnvfDDLIDAKRILR-EIKLLRHLRHENiiGLLDILRPPSPEDFNdv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   91 YVVMQLQGRNLADLRRSQSRGT------FTIsttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYmLDF 164
Cdd:cd07834    80 YIVTELMETDLHKVIKSPQPLTddhiqyFLY--------QILRGLKYLHSANVIHRDLKPSNILVN---SNCDLKI-CDF 147

                  ....*
gi 116812624  165 GLARQ 169
Cdd:cd07834   148 GLARG 152
STKc_PAK1 cd06654
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine ...
10-226 5.92e-12

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 1, 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. PAK1 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). 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.


Pssm-ID: 132985 [Multi-domain]  Cd Length: 296  Bit Score: 66.67  E-value: 5.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   10 ILSVGIlVKERWKVLRKIGGGGFGEIYDALDMLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRND 87
Cdd:cd06654    12 IVSVGD-PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRqMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYLVGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   88 RFNYVVMQLQGRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLa 167
Cdd:cd06654    91 ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVC---RECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF- 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  168 rqftnsCGDVRPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06654   163 ------CAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_p38alpha_MAPK14 cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase; ...
17-223 6.41e-12

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase; Serine/Threonine Kinases (STKs), p38alpha subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta. p38alpha, also called 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.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 67.37  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   17 VKERWKVLRKIGGGGFGEIYDALDMLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCGRNDR 88
Cdd:cd07877    15 VPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKklsrpFQSIIHAKRTYR-ELRLLKHMKHENVIGLldvFTPARSLEE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   89 FN--YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDFGL 166
Cdd:cd07877    94 FNdvYLVTHLMGADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE---DC-ELKILDFGL 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116812624  167 ARQFTNScgdvrppraVAGFRGTVRYAS----IN-AHRNREMgrhdDLWSLFYMLVEFVVGQ 223
Cdd:cd07877   167 ARHTDDE---------MTGYVATRWYRApeimLNwMHYNQTV----DIWSVGCIMAELLTGR 215
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
27-233 6.68e-12

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 65.62  E-value: 6.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   27 IGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVL--KMEVAVLKKL------------QGKDHVcrfigcgrndrf 89
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVlkkKKIIKRKEVEhtLTERNILSRInhpfivklhyafQTEEKL------------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   90 nYVVMQ-LQGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfpstcrkcyML------ 162
Cdd:cd05123    69 -YLVLEyAPGGELFSHL--SKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENI-------------LLdadghi 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  163 ---DFGLARQFTNSCGDVRppravaGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP---------WRKIK 230
Cdd:cd05123   133 kltDFGLAKELSSEGSRTN------TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPfyaedrkeiYEKIL 206

                  ...
gi 116812624  231 DKE 233
Cdd:cd05123   207 KDP 209
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
20-174 6.82e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 65.98  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQPKQVLKmEVAVLKKLqgkDH--VCRFIGC-GRNDRFnY 91
Cdd:cd08215     1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEidlsnMSEKEREDALN-EVKILKKL---NHpnIIKYYESfEEKGKL-C 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   92 VVMQL-QGRNLADL--RRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN---FAMGrfpstcrkcyML--- 162
Cdd:cd08215    76 IVMEYaDGGDLSQKikKQKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNiflTSNG----------LVklg 145
                         170
                  ....*....|..
gi 116812624  163 DFGLARQFTNSC 174
Cdd:cd08215   146 DFGISKVLSSTV 157
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
24-226 8.25e-12

Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related kinase 1; Serine/threonine kinases (STKs), STK25 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). STK25 is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may play a role 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.


Pssm-ID: 132973 [Multi-domain]  Cd Length: 277  Bit Score: 65.84  E-value: 8.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   24 LRKIGGGGFGEIYDALDMLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNDRFNYVVMQ-LQGR 99
Cdd:cd06642     9 LERIGKGSFGEVYKGIDNRTKEVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YITRYYGSYLKGTKLWIIMEyLGGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  100 NLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTnscgDVRP 179
Cdd:cd06642    88 SALDLLKPGPLEETYIATIL---REILKGLDYLHSERKIHRDIKAANVLL----SEQGDVKLADFGVAGQLT----DTQI 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 116812624  180 PRAVagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06642   157 KRNT--FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
22-277 1.09e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 65.41  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   22 KVLRKIGGGGFGEIYDALDMLTRENVALKV-----ESAQQpKQVLkMEVAVLKKLQGKDHVCRFIGCGRNDRFnYVVMQL 96
Cdd:cd06605     4 EYLGELGAGNSGVVSKVLHRPTGKIMAVKTirleiNEAIQ-KQIL-RELDILHKCNSPYIVGFYGAFYNNGDI-SICMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   97 QGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSV-GFLHRDIKPSNFAM---GRFPstcrkcyMLDFGLARQFTN 172
Cdd:cd06605    81 MDGGSLDKILKEVQGRIPERILGKIAVAVLKGLTYLHEKhKIIHRDVKPSNILVnsrGQIK-------LCDFGVSGQLVN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  173 SCGDVrppravagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK-----EQVGSIKERYDHRLM 247
Cdd:cd06605   154 SLAKT--------FVGTSSYMAPERIQGNDYSVKSDIWSLGLSLIELATGRFPYPPENDPpdgifELLQYIVNEPPPRLP 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 116812624  248 LKHLPPEFSIFLDHISSLDYFTKPDYQLLT 277
Cdd:cd06605   226 SGKFSPDFQDFVNLCLIKDPRERPSYKELL 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine ...
22-173 1.17e-11

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9-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. 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. 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.


Pssm-ID: 143345 [Multi-domain]  Cd Length: 287  Bit Score: 65.64  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   22 KVLRKIGGGGFGEIYDALDMLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQgKDHVCRFI----GCGRNDRfnYV 92
Cdd:cd07840     2 EKIAQIGEGTYGQVYKARNKKTGELVALKkirMENEKEgfPITAIR-EIKLLQKLR-HPNIVRLKeivtSKGKGSI--YM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   93 VMQ-----LQGRnladLRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpsTCRKcyML---DF 164
Cdd:cd07840    78 VFEymdhdLTGL----LDSPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILI-----NNDG--VLklaDF 144

                  ....*....
gi 116812624  165 GLARQFTNS 173
Cdd:cd07840   145 GLARPYTKR 153
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
10-226 1.34e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group I, 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 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. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others.


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 65.70  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   10 ILSVGIlVKERWKVLRKIGGGGFGEIYDALDMLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRND 87
Cdd:cd06647    11 IVSVGD-PKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKqMNLQQQPKKELIInEILVMRENKHPNIVNYLDSYLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   88 RFnYVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGL 166
Cdd:cd06647    90 EL-WVVMEyLAGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116812624  167 arqftnsCGDVRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 226
Cdd:cd06647   162 -------CAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; Serine ...
20-179 1.38e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. 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. 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.


Pssm-ID: 173754 [Multi-domain]  Cd Length: 310  Bit Score: 65.86  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   20 RWKVLRKIGGGGFGEIYDALDMLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKD-----HVCRFIGCGRNdRF 89
Cdd:cd07865    13 KYEKLAKIGQGTFGEVFKARHKKTKQIVALKkvlMENEKEgfPITALR-EIKILQLLKHENvvnliEICRTKATPYN-RY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   90 N---YVVMQLQGRNLADLRrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGL 166
Cdd:cd07865    91 KgsfYLVFEFCEHDLAGLL-SNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITK--DGILK--LADFGL 165
                         170
                  ....*....|...
gi 116812624  167 ARQFTNSCGDVRP 179
Cdd:cd07865   166 ARAFSLSKNSKPN 178
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
22-225 1.48e-11

Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ROCK- and NDR-like subfamily, fungal Sid2p- and Dbf2p-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sid2p- and Dbf2p-like group is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 65.89  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   22 KVLRKIGGGGFGEIYDALDMLTRENVALK------VESAQQPKQVLKmEVAVLkkLQGK-DHVCRFIGCGRNDRFNYVVM 94
Cdd:cd05600     4 QILTQVGQGGYGQVFLAKKKDTGEIVALKrmkkslLFKLNEVRHVLT-ERDIL--TTTKsEWLVKLLYAFQDDEYLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   95 Q-LQG-------RNLADLRRSQSRgtFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGL 166
Cdd:cd05600    81 EyVPGgdfrtllNNLGVLSEDHAR--FYMA-------EMFEAVDALHELGYIHRDLKPENFLIDA--SGHIK--LTDFGL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116812624  167 ARQFTNSCGDVrppravagfRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 225
Cdd:cd05600   148 SKGIVTYANSV---------VGSPDYMAPEVLRGKGYDFTVDYWSLGCMLYEFLCGFPP 197
STKc_YSK4 cd06631
Catalytic domain of the Protein Serine/Threonine Kinase, Yeast Sps1/Ste20-related kinase 4; ...
21-256 1.71e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Yeast Sps1/Ste20-related kinase 4; Serine/threonine kinases (STKs), yeast Sps1/Ste20-related kinase 4 (YSK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs (MKKKs or 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.


Pssm-ID: 132962 [Multi-domain]  Cd Length: 265  Bit Score: 64.93  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   21 WKVLRKIGGGGFGEIYDAL----DMLTRENVAL---KVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVV 93
Cdd:cd06631     2 WTKGEVLGKGAYGTVYCGLtnqgQLIAVKQVELdtsNVLAAEKEYEKLQEEVDLLKSLKHVNIVQYLGTCLDDNTISIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   94 MQLQGRNLAD-LRRSqsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKcyMLDFGLARQFTN 172
Cdd:cd06631    82 EFVPGGSISSiLNRF---GPLPEPVFCKYTKQILDGVAYLHNNCVVHRDIKGNNVML--MPNGIIK--LIDFGCARRLAW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  173 SCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIkdkEQVGSIKERYDHRLMLKHLP 252
Cdd:cd06631   155 VGLHGTHSNMLKSMHGTPYWMAPEVINESGYGRKSDIWSIGCTVFEMATGKPPLASM---DRLAAMFYIGAHRGLMPRLP 231

                  ....
gi 116812624  253 PEFS 256
Cdd:cd06631   232 DSFS 235
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; Protein Tyrosine ...
26-254 2.84e-11

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; Protein Tyrosine Kinase (PTK) family; Csk homologous kinase (Chk); 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. Csk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases 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. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). To inhibit Src kinases, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Chk inhibit 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. 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.


Pssm-ID: 133214  Cd Length: 254  Bit Score: 63.82  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   26 KIGGGGFGEIYDAldMLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNDRFnYVVMQLQGR-NLADL 104
Cdd:cd05083    13 IIGEGEFGAVLQG--EYTGQKVAVKNIKCDVTAQAFLEETAVMTKLHHKNLV-RLLGVILHNGL-YIVMELMSKgNLVNF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624  105 RRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQftnscgdvrPPRAVA 184
Cdd:cd05083    89 LRTRGRALVSVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILV----SEDGVAKVSDFGLARV---------GSMGVD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116812624  185 GFRGTVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKERYdhrlmlKHLPPE 254
Cdd:cd05083   156 NSKLPVKWTAPEALKHKKFSSKSDVWSYGVLLWEvFSYGRAPYPKMSLKEVKECVEKGY------RMEPPE 220
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; Serine ...
19-170 4.41e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; Serine/Threonine Kinases (STKs), Cell Division Cycle 2-like 1 (CDC2L1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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).


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 63.78  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812624   19 ERWKVLRKIGGGGFGEIYDALDML