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Conserved domains on  [gi|119628251|gb|EAX07846|]
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PDLIM1 interacting kinase 1 like, isoform CRA_a [Homo sapiens]

Protein Classification

PDIK1L family serine/threonine-protein kinase( domain architecture ID 10195580)

PDIK1L (PDLIM1-interacting kinase 1-like) family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
7-331 0e+00

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


:

Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 633.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSH 86
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEECVLQRDGLAQRMSH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSS-LYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd13977   81 GSSKSdLYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdlEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGI 245
Cdd:cd13977  161 KPDNILISHKRG-----EPILKVADFGLSKVCSGSGLNPEEPANVNKHFLSSACGSDFYMAPEVWEGHYTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 IIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKK-SMNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd13977  236 IIWAMVERITFRDGETKKELLGTYIQQGKEIVPLGEALLENPKLELQIPLKKKkSMNDDMKQLLRDMLAANPQERPDAFQ 315

                 ....*..
gi 119628251 325 LELRLVQ 331
Cdd:cd13977  316 LELRLRQ 322
 
Name Accession Description Interval E-value
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
7-331 0e+00

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 633.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSH 86
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEECVLQRDGLAQRMSH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSS-LYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd13977   81 GSSKSdLYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdlEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGI 245
Cdd:cd13977  161 KPDNILISHKRG-----EPILKVADFGLSKVCSGSGLNPEEPANVNKHFLSSACGSDFYMAPEVWEGHYTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 IIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKK-SMNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd13977  236 IIWAMVERITFRDGETKKELLGTYIQQGKEIVPLGEALLENPKLELQIPLKKKkSMNDDMKQLLRDMLAANPQERPDAFQ 315

                 ....*..
gi 119628251 325 LELRLVQ 331
Cdd:cd13977  316 LELRLRQ 322
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
8-325 1.16e-61

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 197.37  E-value: 1.16e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251     8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmsh 86
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKkKIKKDRERILREIKILKKLK--HPNIVRLYDVFEDED-------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    87 gsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:smart00220  71 ---------------------------KLYLVMEYCEGGDLFDLLKKRGRlSEDEARFYLRQILSALEYLHSKGIVHRDL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   166 KPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEG-HYTAKADIFALG 244
Cdd:smart00220 124 KPENILL--------DEDGHVKLADFGLARQLDPGE------------KLTTFVGTPEYMAPEVLLGkGYGKAVDIWSLG 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   245 IIIWAMLE-RITFIDTETKKELLgsyvkqgteivpvgeALLENPKMELLIPVKKKSMNgrMKQLIKEMLAANPQDRPDAF 323
Cdd:smart00220 184 VILYELLTgKPPFPGDDQLLELF---------------KKIGKPKPPFPPPEWDISPE--AKDLIRKLLVKDPEKRLTAE 246

                   ..
gi 119628251   324 EL 325
Cdd:smart00220 247 EA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
7-333 7.20e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.79  E-value: 7.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR---CHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqk 83
Cdd:COG0515    8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARL--NHPNIVRVYD----------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:COG0515   75 ----------------------VGEEDGRPYL--VMEYVEGESLADLLRRRGPlPPAEALRILAQLAEALAAAHAAGIVH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsdlepTLKVADFGLSKVcsASGQNPEEPvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:COG0515  131 RDIKPANILLTPDG--------RVKLIDFGIARA--LGGATLTQT--------GTVVGTPGYMAPEQARGEpVDPRSDVY 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLGSYVKQgtEIVPVGEALLENPkmellipvkkksmnGRMKQLIKEMLAANPQDRP- 320
Cdd:COG0515  193 SLGVTLYELLTGRPPFDGDSPAELLRAHLRE--PPPPPSELRPDLP--------------PALDAIVLRALAKDPEERYq 256
                        330
                 ....*....|...
gi 119628251 321 DAFELELRLVQIA 333
Cdd:COG0515  257 SAAELAAALRAVL 269
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
10-248 9.75e-30

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 114.13  E-value: 9.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   10 LIREVGRGSYGVVYEAVIR----KTSARVAVKKIRCHAPENvelALREFWALSSI--KSQHPNVIHLEECILQKDgmvqk 83
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKgegeNTKIKVAVKTLKEGADEE---EREDFLEEASImkKLDHPNIVKLLGVCTQGE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   84 mshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQII 161
Cdd:pfam07714  75 ------------------------------PLYIVTEYMPGGDLLDFLRKHKRKLTLKDllSMALQIAKGMEYLESKNFV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  162 HRDLKPDNILISQTRldtsdlepTLKVADFGLSKVcsasGQNPEEPVSVNKCFLSTacgtdFYMAPEVW-EGHYTAKADI 240
Cdd:pfam07714 125 HRDLAARNCLVSENL--------VVKISDFGLSRD----IYDDDYYRKRGGGKLPI-----KWMAPESLkDGKFTSKSDV 187

                  ....*...
gi 119628251  241 FALGIIIW 248
Cdd:pfam07714 188 WSFGVLLW 195
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
3-251 1.26e-19

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 89.32  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   3 SSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapENVELALREFWALSSIksQHPNVIHLeecilqKDGMVQ 82
Cdd:PTZ00036  63 SPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVL----QDPQYKNRELLIMKNL--NHINIIFL------KDYYYT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVetslkgeIAFDPRSAYylwfvmdfcdggdmnEYLLSRKPNRKTNTSFML-----QLSSALAFLHK 157
Cdd:PTZ00036 131 ECFKKNEKNIFLNVV-------MEFIPQTVH---------------KYMKHYARNNHALPLFLVklysyQLCRALAYIHS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrldtsdlEP---TLKVADFGLSKVCSAsGQNPeepvsvnkcfLSTACgTDFYMAPEVWEG-- 232
Cdd:PTZ00036 189 KFICHRDLKPQNLLI----------DPnthTLKLCDFGSAKNLLA-GQRS----------VSYIC-SRFYRAPELMLGat 246
                        250
                 ....*....|....*....
gi 119628251 233 HYTAKADIFALGIIIWAML 251
Cdd:PTZ00036 247 NYTTHIDLWSLGCIIAEMI 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
113-251 1.22e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.77  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 113 YYLwfVMDFCDGGDMNEYLLSRKP--NRKTnTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVAD 190
Cdd:NF033483  82 PYI--VMEYVDGRTLKDYIREHGPlsPEEA-VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDG--------RVKVTD 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 191 FGLSKVCSASG--QNpeepvsvnkcflSTACGTDFYMAPEVWEGHY-TAKADIFALGIIIWAML 251
Cdd:NF033483 151 FGIARALSSTTmtQT------------NSVLGTVHYLSPEQARGGTvDARSDIYSLGIVLYEML 202
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
30-319 2.78e-14

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 74.11  E-value: 2.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    30 TSARVAVKKIRCHAPENVELALReFWALSSIKSQ--HPNVIHLEECILQKDGMvqkmshgsnsslylqlvetslkgeiaf 107
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRAR-FRRETALCARlyHPNIVALLDSGEAPPGL--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   108 dprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNT-SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTrldtsDLEPTL 186
Cdd:TIGR03903   54 -------LFAVFEYVPGRTLREVLAADGALPAGETgRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQT-----GVRPHA 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   187 KVADFGLSKVCSASGQNPEEPVSVNKCFLstacGTDFYMAPEVWEGH-YTAKADIFALGIIIwamLERITfidtetkkel 265
Cdd:TIGR03903  122 KVLDFGIGTLLPGVRDADVATLTRTTEVL----GTPTYCAPEQLRGEpVTPNSDLYAWGLIF---LECLT---------- 184
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251   266 lGSYVKQGTEIVPVGEALLeNPkMELLIPvkkKSMNG-RMKQLIKEMLAANPQDR 319
Cdd:TIGR03903  185 -GQRVVQGASVAEILYQQL-SP-VDVSLP---PWIAGhPLGQVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
7-331 0e+00

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 633.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSH 86
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEECVLQRDGLAQRMSH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSS-LYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd13977   81 GSSKSdLYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdlEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGI 245
Cdd:cd13977  161 KPDNILISHKRG-----EPILKVADFGLSKVCSGSGLNPEEPANVNKHFLSSACGSDFYMAPEVWEGHYTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 IIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKK-SMNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd13977  236 IIWAMVERITFRDGETKKELLGTYIQQGKEIVPLGEALLENPKLELQIPLKKKkSMNDDMKQLLRDMLAANPQERPDAFQ 315

                 ....*..
gi 119628251 325 LELRLVQ 331
Cdd:cd13977  316 LELRLRQ 322
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
8-325 1.16e-61

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 197.37  E-value: 1.16e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251     8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmsh 86
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKkKIKKDRERILREIKILKKLK--HPNIVRLYDVFEDED-------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    87 gsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:smart00220  71 ---------------------------KLYLVMEYCEGGDLFDLLKKRGRlSEDEARFYLRQILSALEYLHSKGIVHRDL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   166 KPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEG-HYTAKADIFALG 244
Cdd:smart00220 124 KPENILL--------DEDGHVKLADFGLARQLDPGE------------KLTTFVGTPEYMAPEVLLGkGYGKAVDIWSLG 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   245 IIIWAMLE-RITFIDTETKKELLgsyvkqgteivpvgeALLENPKMELLIPVKKKSMNgrMKQLIKEMLAANPQDRPDAF 323
Cdd:smart00220 184 VILYELLTgKPPFPGDDQLLELF---------------KKIGKPKPPFPPPEWDISPE--AKDLIRKLLVKDPEKRLTAE 246

                   ..
gi 119628251   324 EL 325
Cdd:smart00220 247 EA 248
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
7-251 8.79e-51

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 169.58  E-value: 8.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRL--DHPNIVKLYE------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05117   67 ---------------------VFEDDKNLYL--VMELCTGGELFDRIVKKGSfSEREAAKIMKQILSAVAYLHSQGIVHR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILisqtrLDTSDLEPTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05117  124 DLKPENIL-----LASKDPDSPIKIIDFGLAKIFE------------EGEKLKTVCGTPYYVAPEVLKGKgYGKKCDIWS 186

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd05117  187 LGVILYILL 195
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
7-328 1.64e-50

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 168.92  E-value: 1.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSSIksQHPNVIHLeecilqkdgmvqk 83
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaedEEFRERFLREARALARL--SHPNIVRV------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslYlqlvetslkgEIAFDPRSAYYlwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd14014   66 ---------Y----------DVGEDDGRPYI---VMEYVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRAGIVH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEepvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd14014  124 RDIKPANILLTE--------DGRVKLTDFGIARALGDSGLTQT----------GSVLGTPAYMAPEQARGGpVDPRSDIY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLgsYVKQGTEIVPvgeallenpkmellIPVKKKSMNGRMKQLIKEMLAANPQDRP- 320
Cdd:cd14014  186 SLGVVLYELLTGRPPFDGDSPAAVL--AKHLQEAPPP--------------PSPLNPDVPPALDAIILRALAKDPEERPq 249
                        330
                 ....*....|
gi 119628251 321 --DAFELELR 328
Cdd:cd14014  250 saAELLAALR 259
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
15-325 9.63e-50

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 165.52  E-value: 9.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmshgsnssly 93
Cdd:cd00180    2 GKGSFGKVYKARDKETGKKVAVKVIPKeKLKKLLEELLREIEILKKLN--HPNIVKLYDVFETEN--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd00180   65 --------------------FLYLVMEYCEGGSLKDLLKENKGPLSEEEalSILRQLLSALEYLHSNGIIHRDLKPENIL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 IsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsvNKCFLSTACGTDFYMAPEV-WEGHYTAKADIFALGIIIWAM 250
Cdd:cd00180  125 L--------DSDGTVKLADFGLAKDLDSDD---------SLLKTTGGTTPPYYAPPELlGGRYYGPKVDIWSLGVILYEL 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 251 LEritfidtetkkellgsyvkqgteivpvgeallenpkmellipvkkksmngrMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd00180  188 EE---------------------------------------------------LKDLIRRMLQYDPKKRPSAKEL 211
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
7-325 1.70e-49

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 166.10  E-value: 1.70e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA--PENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkm 84
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmsEKEREEALNEVKLLSKLK--HPNIVKYYESFEENG------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNT-----SFMLQLSSALAFLHKNQ 159
Cdd:cd08215   73 -----------------------------KLCIVMEYADGGDLAQKIKKQKKKGQPFPeeqilDWFVQICLALKYLHSRK 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKA 238
Cdd:cd08215  124 ILHRDLKTQNIFLTKDG--------VVKLGDFGISKVLESTTD-----------LAKTVVGTPYYLSPELCENKpYNYKS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIW--AMLERiTFiDTETKKELLGSYVKQGTEIVPvgeallenpkmellipvkkKSMNGRMKQLIKEMLAANP 316
Cdd:cd08215  185 DIWALGCVLYelCTLKH-PF-EANNLPALVYKIVKGQYPPIP-------------------SQYSSELRDLVNSMLQKDP 243

                 ....*....
gi 119628251 317 QDRPDAFEL 325
Cdd:cd08215  244 EKRPSANEI 252
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
14-251 9.81e-47

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 158.92  E-value: 9.81e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmshgsnsS 91
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKklNKKLQENLESEIAILKSIK--HPNIVRLYDVQKTED------------F 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 LYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd14009   67 IYL-----------------------VLEYCAGGDLSQYIRKRGRlPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LisqtrLDTSDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWA 249
Cdd:cd14009  124 L-----LSTSGDDPVLKIADFGFARSLQPAS------------MAETLCGSPLYMAPEILQFQkYDAKADLWSVGAILFE 186

                 ..
gi 119628251 250 ML 251
Cdd:cd14009  187 ML 188
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
14-321 1.46e-45

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 155.39  E-value: 1.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSarVAVKKIRCHA--PENVELALREFWALSSIKsqHPNVIhleecilqkdgmvqkmshgsnss 91
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTD--VAIKKLKVEDdnDELLKEFRREVSILSKLR--HPNIV----------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetSLKGEIAFDPRsayyLWFVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd13999   54 --------QFIGACLSPPP----LCIVTEYMPGGSLYDLLHKKKIplSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILIsqtrldtsDLEPTLKVADFGLSKVcsasgqnpeepVSVNKCFLSTACGTDFYMAPEVWEG-HYTAKADIFALGIIIW 248
Cdd:cd13999  122 ILL--------DENFTVKIADFGLSRI-----------KNSTTEKMTGVVGTPRWMAPEVLRGePYTEKADVYSFGIVLW 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 249 AMLER-ITFidtetkKELlgSYVKQGTEIVPVGEallenpkmELLIPvkkKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd13999  183 ELLTGeVPF------KEL--SPIQIAAAVVQKGL--------RPPIP---PDCPPELSKLIKRCWNEDPEKRPS 237
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
7-320 1.47e-45

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 155.75  E-value: 1.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHAPENVElalREFWALSSIksQHPNVIHLEECILQKDgmv 81
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidksKLKEEIEEKIK---REIEIMKLL--NHPNIIKLYEVIETEN--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd14003   73 --------------------------------KIYLVMEYASGGELFDYIVNNGRlSEDEARRFFQQLISAVDYCHSNGI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEGH--YTAKA 238
Cdd:cd14003  121 VHRDLKLENILL--------DKNGNLKIIDFGLSNEFR------------GGSLLKTFCGTPAYAAPEVLLGRkyDGPKA 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAMLE-RITFIDTETKKelLGSYVKQGTEIVPvgeallenpkmellipvkkKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd14003  181 DVWSLGVILYAMLTgYLPFDDDNDSK--LFRKILKGKYPIP-------------------SHLSPDARDLIRRMLVVDPS 239

                 ...
gi 119628251 318 DRP 320
Cdd:cd14003  240 KRI 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
7-333 7.20e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.79  E-value: 7.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR---CHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqk 83
Cdd:COG0515    8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelAADPEARERFRREARALARL--NHPNIVRVYD----------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:COG0515   75 ----------------------VGEEDGRPYL--VMEYVEGESLADLLRRRGPlPPAEALRILAQLAEALAAAHAAGIVH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsdlepTLKVADFGLSKVcsASGQNPEEPvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:COG0515  131 RDIKPANILLTPDG--------RVKLIDFGIARA--LGGATLTQT--------GTVVGTPGYMAPEQARGEpVDPRSDVY 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLGSYVKQgtEIVPVGEALLENPkmellipvkkksmnGRMKQLIKEMLAANPQDRP- 320
Cdd:COG0515  193 SLGVTLYELLTGRPPFDGDSPAELLRAHLRE--PPPPPSELRPDLP--------------PALDAIVLRALAKDPEERYq 256
                        330
                 ....*....|...
gi 119628251 321 DAFELELRLVQIA 333
Cdd:COG0515  257 SAAELAAALRAVL 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
7-253 2.13e-42

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 147.73  E-value: 2.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmsh 86
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCK--HPNIVKYYGSYLKKD-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSR-KPNRKTNTSF-MLQLSSALAFLHKNQIIHRD 164
Cdd:cd05122   71 ---------------------------ELWIVMEFCSGGSLKDLLKNTnKTLTEQQIAYvCKEVLKGLEYLHSHGIIHRD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILIsqtrldTSDLEptLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEG-HYTAKADIFAL 243
Cdd:cd05122  124 IKAANILL------TSDGE--VKLIDFGLSAQLS------------DGKTRNTFVGTPYWMAPEVIQGkPYGFKADIWSL 183
                        250
                 ....*....|
gi 119628251 244 GIIIWAMLER 253
Cdd:cd05122  184 GITAIEMAEG 193
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
11-325 1.40e-41

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 145.90  E-value: 1.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCH-APENVELALREFWALSSIksQHPNVIHLEECILQKDgmvqkmshgsn 89
Cdd:cd13996   11 IELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTeKSSASEKVLREVKALAKL--NHPNIVRYYTAWVEEP----------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sSLYLQlvetslkgeiafdprsayylwfvMDFCDGGDMNEYLLSR----KPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd13996   78 -PLYIQ-----------------------MELCEGGTLRDWIDRRnsssKNDRKLALELFKQILKGVSYIHSKGIVHRDL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdlepTLKVADFGLskVCSASGQNPEEPVSVNKCF-----LSTACGTDFYMAPEVWEG-HYTAKAD 239
Cdd:cd13996  134 KPSNIFLDNDDL-------QVKIGDFGL--ATSIGNQKRELNNLNNNNNgntsnNSVGIGTPLYASPEQLDGeNYNEKAD 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAML-------ERITFIDTetkkellgsyVKQGteIVPVgEALLENPKmellipvkkksmngrMKQLIKEML 312
Cdd:cd13996  205 IYSLGIILFEMLhpfktamERSTILTD----------LRNG--ILPE-SFKAKHPK---------------EADLIQSLL 256
                        330
                 ....*....|...
gi 119628251 313 AANPQDRPDAFEL 325
Cdd:cd13996  257 SKNPEERPSAEQL 269
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
8-325 1.31e-37

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 135.05  E-value: 1.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENvELALREFWALSSIKS--QHPNVIHLEEcilqkdgmvqkms 85
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHP-KAALREIKLLKHLNDveGHPNIVKLLD------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiAFDPRSAYYLWFVMDFCDggdMNEYLLSRKPNRKTN----TSFMLQLSSALAFLHKNQII 161
Cdd:cd05118   67 --------------------VFEHRGGNHLCLVFELMG---MNLYELIKDYPRGLPldliKSYLYQLLQALDFLHSNGII 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRldtsdlePTLKVADFGLSkvCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKAD 239
Cdd:cd05118  124 HRDLKPENILINLEL-------GQLKLADFGLA--RSFTSPPYTPYVA-----------TRWYRAPEVLLGakPYGSSID 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERITFIDTEtkkellgSYVKQGTEIVpvgeALLENPKmellipvkkksmngrMKQLIKEMLAANPQDR 319
Cdd:cd05118  184 IWSLGCILAELLTGRPLFPGD-------SEVDQLAKIV----RLLGTPE---------------ALDLLSKMLKYDPAKR 237

                 ....*.
gi 119628251 320 PDAFEL 325
Cdd:cd05118  238 ITASQA 243
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
7-246 2.02e-35

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 129.78  E-value: 2.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL-------ALREFwALSSIKSQHPNVIHLEEcilqkdg 79
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGndfqklpQLREI-DLHRRVSRHPNIITLHD------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 mvqkmshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNT---SFMLQLSSALAFLH 156
Cdd:cd13993   73 --------------------------VFETEVAIYI--VLEYCPNGDLFEAITENRIYVGKTElikNVFLQLIDAVKHCH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTrldtsdlEPTLKVADFGLSKvcsasgqnpEEPVSVNKCflstaCGTDFYMAPEVW------ 230
Cdd:cd13993  125 SLGIYHRDIKPENILLSQD-------EGTVKLCDFGLAT---------TEKISMDFG-----VGSEFYMAPECFdevgrs 183
                        250
                 ....*....|....*..
gi 119628251 231 -EGHYTAKADIFALGII 246
Cdd:cd13993  184 lKGYPCAAGDIWSLGII 200
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
8-251 3.44e-34

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 126.51  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHA-PENVELALREFWALSSIKSQHpnVIHLEEcilqkdgmvqkms 85
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKInREKAgSSAVKLLEREVDILKHVNHAH--IIHLEE------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqLVETSLKgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHRD 164
Cdd:cd14097   68 ----------VFETPKR------------MYLVMELCEDGELKELLLRKGFFSENETRHIIQsLASAVAYLHKNDIVHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTRLDTSDlEPTLKVADFGLSKVCSASGQNpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIFAL 243
Cdd:cd14097  126 LKLENILVKSSIIDNND-KLNIKVTDFGLSVQKYGLGED----------MLQETCGTPIYMAPEVISAHgYSQQCDIWSI 194

                 ....*...
gi 119628251 244 GIIIWAML 251
Cdd:cd14097  195 GVIMYMLL 202
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
8-320 5.93e-34

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 125.76  E-value: 5.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTS--ARVAVKKI-RCHAPEN-VELAL-REFWALSSIKsqHPNVIHLEEcILQKDGMVq 82
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKIIdKKKAPKDfLEKFLpRELEILRKLR--HPNIIQVYS-IFERGSKV- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetslkgeiafdprsayylWFVMDFCDGGDMNEYLLSRK--PNRKTNTsFMLQLSSALAFLHKNQI 160
Cdd:cd14080   78 ---------------------------------FIFMEYAEHGDLLEYIQKRGalSESQARI-WFRQLALAVQYLHSLDI 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSaSGQNPEepvsvnkcfLS-TACGTDFYMAPEVWEGH-YTAK- 237
Cdd:cd14080  124 AHRDLKCENILLDSNN--------NVKLSDFGFARLCP-DDDGDV---------LSkTFCGSAAYAAPEILQGIpYDPKk 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAML-ERITFIDTETKKellgsyvkqgteivpvgeaLLENPKM-ELLIPVKKKSMNGRMKQLIKEMLAAN 315
Cdd:cd14080  186 YDIWSLGVILYIMLcGSMPFDDSNIKK-------------------MLKDQQNrKVRFPSSVKKLSPECKDLIDQLLEPD 246

                 ....*
gi 119628251 316 PQDRP 320
Cdd:cd14080  247 PTKRA 251
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
8-251 7.58e-34

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 124.89  E-value: 7.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHapENVELALREfwalssIKSQ----HPNVIHLeecilqkd 78
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKvisksQLQKS--GLEHQLRRE------IEIQshlrHPNILRL-------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkmsHGS---NSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAF 154
Cdd:cd14007   66 -------YGYfedKKRIYL-----------------------ILEYAPNGELYKELKKQKRfDEKEAAKYIYQLALALDY 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNpeepvsvnkcflsTACGTDFYMAPEVWEG-H 233
Cdd:cd14007  116 LHSKNIIHRDIKPENILL--------GSNGELKLADFGWSVHAPSNRRK-------------TFCGTLDYLPPEMVEGkE 174
                        250
                 ....*....|....*...
gi 119628251 234 YTAKADIFALGIIIWAML 251
Cdd:cd14007  175 YDYKVDIWSLGVLCYELL 192
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
8-325 1.49e-33

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 124.95  E-value: 1.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVeLALREFWALSSIKSqHPNVIHLEECILQKDgmvqkms 85
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMkkKFYSWEEC-MNLREVKSLRKLNE-HPNIVKLKEVFREND------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGgdmNEYLLSRKPNRKTNT-----SFMLQLSSALAFLHKNQI 160
Cdd:cd07830   72 ----------------------------ELYFVFEYMEG---NLYQLMKDRKGKPFSesvirSIIYQILQGLAHIHKHGF 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRldtsdlepTLKVADFGLSK-VCSasgQNP-EEPVSvnkcflstacgTDFYMAPEVW--EGHYTA 236
Cdd:cd07830  121 FHRDLKPENLLVSGPE--------VVKIADFGLAReIRS---RPPyTDYVS-----------TRWYRAPEILlrSTSYSS 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIiwaMLERITF---------IDTETKK-ELLGSYVKQgteIVPVGEALLEnpKMELLIP-VKKKSMNGRMK 305
Cdd:cd07830  179 PVDIWALGCI---MAELYTLrplfpgsseIDQLYKIcSVLGTPTKQ---DWPEGYKLAS--KLGFRFPqFAPTSLHQLIP 250
                        330       340
                 ....*....|....*....|....*..
gi 119628251 306 -------QLIKEMLAANPQDRPDAFEL 325
Cdd:cd07830  251 naspeaiDLIKDMLRWDPKKRPTASQA 277
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
8-325 2.93e-33

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 124.01  E-value: 2.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI---RChaPENVELALREFWALSSIksQHPNVIHleecilqkdgmvqkm 84
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIdleKC--QTSMDELRKEIQAMSQC--NHPNVVS--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNsslylqLVETSLkgeiafdprsayylWFVMDFCDGGDMNEYLLSRKPN----RKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd06610   64 YYTSF------VVGDEL--------------WLVMPLLSGGSLLDIMKSSYPRggldEAIIATVLKEVLKGLEYLHSNGQ 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEpvsVNKCFLSTACgtdfYMAPEVWEGH--YTAKA 238
Cdd:cd06610  124 IHRDVKAGNILLGE--------DGSVKIADFGVSASLATGGDRTRK---VRKTFVGTPC----WMAPEVMEQVrgYDFKA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGiiiwamlerITFIDTETKKELLGSYvkqgteivPVGEAL---LENPKMELLIPVKKKSMNGRMKQLIKEMLAAN 315
Cdd:cd06610  189 DIWSFG---------ITAIELATGAAPYSKY--------PPMKVLmltLQNDPPSLETGADYKKYSKSFRKMISLCLQKD 251
                        330
                 ....*....|
gi 119628251 316 PQDRPDAFEL 325
Cdd:cd06610  252 PSKRPTAEEL 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7-332 3.25e-33

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 123.81  E-value: 3.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEaVIRKTSARV-AVKKIRCHAPENVE--LALREFWALSSIKsqHPNVIHLEECILQKdgmvqk 83
Cdd:cd08217    1 DYEVLETIGKGSFGTVRK-VRRKSDGKIlVWKEIDYGKMSEKEkqQLVSEVNILRELK--HPNIVRYYDRIVDR------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLlsrKPNRKTNT--------SFMLQLSSALAFL 155
Cdd:cd08217   72 ----ANTTLYI-----------------------VMEYCEGGDLAQLI---KKCKKENQyipeefiwKIFTQLLLALYEC 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 H-----KNQIIHRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVW 230
Cdd:cd08217  122 HnrsvgGGKILHRDLKPANIFLDSD--------NNVKLGDFGLARVLSHDSS-----------FAKTYVGTPYYMSPELL 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 231 EGH-YTAKADIFALGIIIWAMLERITFIDTETKKElLGSYVKQGTeivpvgeallENPkmellIPVKKKSmngRMKQLIK 309
Cdd:cd08217  183 NEQsYDEKSDIWSLGCLIYELCALHPPFQAANQLE-LAKKIKEGK----------FPR-----IPSRYSS---ELNEVIK 243
                        330       340
                 ....*....|....*....|...
gi 119628251 310 EMLAANPQDRPDAFELeLRLVQI 332
Cdd:cd08217  244 SMLNVDPDKRPSVEEL-LQLPLI 265
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
10-329 4.71e-33

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 123.04  E-value: 4.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    10 LIREVGRGSYGVVYEAVIRKTSA----RVAVKKIRCHA-PENVELALREFWALSSIksQHPNVIHLEECILQKDGmvqkm 84
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTLKGKGDgkevEVAVKTLKEDAsEQQIEEFLREARIMRKL--DHPNIVKLLGVCTEEEP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    85 shgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNR---KTNTSFMLQLSSALAFLHKNQII 161
Cdd:smart00221  76 ------------------------------LMIVMEYMPGGDLLDYLRKNRPKElslSDLLSFALQIARGMEYLESKNFI 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   162 HRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASG----QNPEEPVsvnkcflstacgtdFYMAPEVW-EGHYTA 236
Cdd:smart00221 126 HRDLAARNCLVGENL--------VVKISDFGLSRDLYDDDyykvKGGKLPI--------------RWMAPESLkEGKFTS 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   237 KADIFALGIIIWAMLeriTFIDT----ETKKELLgSYVKQGteivpvgeALLENPkmellipvkkKSMNGRMKQLIKEML 312
Cdd:smart00221 184 KSDVWSFGVLLWEIF---TLGEEpypgMSNAEVL-EYLKKG--------YRLPKP----------PNCPPELYKLMLQCW 241
                          330
                   ....*....|....*..
gi 119628251   313 AANPQDRPDAFELELRL 329
Cdd:smart00221 242 AEDPEDRPTFSELVEIL 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
7-245 9.42e-33

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 122.74  E-value: 9.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKSqhPNVIHLEECILqkdgmvqkms 85
Cdd:cd06609    2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLeEAEDEIEDIQQEIQFLSQCDS--PYITKYYGSFL---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSNsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd06609   70 KGSK-------------------------LWIIMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDI 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLskvcsaSGQnpeepVSVNKCFLSTACGTDFYMAPEV-WEGHYTAKADIFALG 244
Cdd:cd06609  125 KAANILLSE--------EGDVKLADFGV------SGQ-----LTSTMSKRNTFVGTPFWMAPEViKQSGYDEKADIWSLG 185

                 .
gi 119628251 245 I 245
Cdd:cd06609  186 I 186
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
10-329 9.58e-33

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 122.25  E-value: 9.58e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    10 LIREVGRGSYGVVYEAVIR----KTSARVAVKKIRCHA-PENVELALREFWALSSIksQHPNVIHLEECILQKDGmvqkm 84
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKgkggKKKVEVAVKTLKEDAsEQQIEEFLREARIMRKL--DHPNVVKLLGVCTEEEP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    85 shgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIH 162
Cdd:smart00219  76 ------------------------------LYIVMEYMEGGDLLSYLRKNRPKLSLSDllSFALQIARGMEYLESKNFIH 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   163 RDLKPDNILISQTRldtsdlepTLKVADFGLSKVCS----ASGQNPEEPVsvnkcflstacgtdFYMAPEVW-EGHYTAK 237
Cdd:smart00219 126 RDLAARNCLVGENL--------VVKISDFGLSRDLYdddyYRKRGGKLPI--------------RWMAPESLkEGKFTSK 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   238 ADIFALGIIIWAMLeriTFIDT----ETKKELLgSYVKQGteivpvgeallenpkMELLIPvkkKSMNGRMKQLIKEMLA 313
Cdd:smart00219 184 SDVWSFGVLLWEIF---TLGEQpypgMSNEEVL-EYLKNG---------------YRLPQP---PNCPPELYDLMLQCWA 241
                          330
                   ....*....|....*.
gi 119628251   314 ANPQDRPDAFELELRL 329
Cdd:smart00219 242 EDPEDRPTFSELVEIL 257
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
14-326 2.65e-32

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 121.00  E-value: 2.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIrcHAPENVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkmsHGSNSSly 93
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKII--ESESEKKAFEVEVRQLSRVD--HPNIIKL---------------YGACSN-- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdpRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNT----SFMLQLSSALAFLHKNQ---IIHRDLK 166
Cdd:cd14058   58 ----------------QKPVCL--VMEYAEGGSLYNVLHGKEPKPIYTAahamSWALQCAKGVAYLHSMKpkaLIHRDLK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRLDtsdleptLKVADFGLskVCSASGQnpeepVSVNKcflstacGTDFYMAPEVWEG-HYTAKADIFALGI 245
Cdd:cd14058  120 PPNLLLTNGGTV-------LKICDFGT--ACDISTH-----MTNNK-------GSAAWMAPEVFEGsKYSEKCDVFSWGI 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 IIWAMLERitfidTETKKELLGSYVKQgTEIVPVGeallENPKMELLIPvkkksmnGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14058  179 ILWEVITR-----RKPFDHIGGPAFRI-MWAVHNG----ERPPLIKNCP-------KPIESLMTRCWSKDPEKRPSMKEI 241

                 .
gi 119628251 326 E 326
Cdd:cd14058  242 V 242
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
7-251 3.00e-32

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 120.89  E-value: 3.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRC----HAPENvELALrefwaLSSIKsqHPNVIHLEEcilqkdg 79
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKiidKAKCkgkeHMIEN-EVAI-----LRRVK--HPNIVQLIE------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 mvqkmSHGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYL-LSRKPNRKTNTSFMLQLSSALAFLHKN 158
Cdd:cd14095   66 -----EYDTDTELYL-----------------------VMELVKGGDLFDAItSSTKFTERDASRMVTDLAQALKYLHSL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCsasgqnpEEPvsvnkcfLSTACGTDFYMAPEVW-EGHYTAK 237
Cdd:cd14095  118 SIVHRDIKPENLLV----VEHEDGSKSLKLADFGLATEV-------KEP-------LFTVCGTPTYVAPEILaETGYGLK 179
                        250
                 ....*....|....
gi 119628251 238 ADIFALGIIIWAML 251
Cdd:cd14095  180 VDIWAAGVITYILL 193
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
7-322 4.55e-32

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 121.52  E-value: 4.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVE-----LALREFWALSSIKsqHPNVIHLEECIlqkdgmv 81
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdginfTALREIKLLQELK--HPNIIGLLDVF------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmSHGSNSSLylqlvetslkgeiafdprsayylwfVMDFCDGgDMnEYLLSRKPNRKTNT---SFMLQLSSALAFLHKN 158
Cdd:cd07841   72 ---GHKSNINL-------------------------VFEFMET-DL-EKVIKDKSIVLTPAdikSYMLMTLRGLEYLHSN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTA 236
Cdd:cd07841  122 WILHRDLKPNNLLIAS--------DGVLKLADFGLARSFGSPNRK-----------MTHQVVTRWYRAPELLFGarHYGV 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMLERITFIDTETKKELLGS-YVKQGTeivPvGEAllENPKMELL------IPVKKKSMNGRMKQ--- 306
Cdd:cd07841  183 GVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKiFEALGT---P-TEE--NWPGVTSLpdyvefKPFPPTPLKQIFPAasd 256
                        330       340
                 ....*....|....*....|
gi 119628251 307 ----LIKEMLAANPQDRPDA 322
Cdd:cd07841  257 daldLLQRLLTLNPNKRITA 276
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
8-324 5.30e-32

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 121.05  E-value: 5.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR-CHAPENV-ELALREFWALSSIKsqHPNVIHLEECILqkdgmvqkms 85
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRlDNEEEGIpSTALREISLLKELK--HPNIVKLLDVIH---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHR 163
Cdd:cd07829   69 --TENKLYL-----------------------VFEYCDQ-DLKKYLDKRPGPLPPNLikSIMYQLLRGLAYCHSHRILHR 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSaSGQNPEEPVSVnkcflstacgTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd07829  123 DLKPQNLLI--------NRDGVLKLADFGLARAFG-IPLRTYTHEVV----------TLWYRAPEILLGskHYSTAVDIW 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIiwaMLERITF---------IDTETKK-ELLG----------SYVKQGTEIVPVGEAlleNPKMELLipvkkKSMN 301
Cdd:cd07829  184 SVGCI---FAELITGkplfpgdseIDQLFKIfQILGtpteeswpgvTKLPDYKPTFPKWPK---NDLEKVL-----PRLD 252
                        330       340
                 ....*....|....*....|...
gi 119628251 302 GRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd07829  253 PEGIDLLSKMLQYNPAKRISAKE 275
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
12-251 9.11e-32

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 119.55  E-value: 9.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELA--LREFWALSSIksQHPNVIHleeCIlqkdGmvqkmSHGSN 89
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEalEREIRILSSL--KHPNIVR---YL----G-----TERTE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 SSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEyLLSR--KPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd06606   72 NTLNI-----------------------FLEYVPGGSLAS-LLKKfgKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQTRldtsdlepTLKVADFGLSKVCSASGQNpeepvsvnkCFLSTACGTDFYMAPEVWEG-HYTAKADIFALGII 246
Cdd:cd06606  128 ANILVDSDG--------VVKLADFGCAKRLAEIATG---------EGTKSLRGTPYWMAPEVIRGeGYGRAADIWSLGCT 190

                 ....*
gi 119628251 247 IWAML 251
Cdd:cd06606  191 VIEMA 195
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
12-329 2.20e-31

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 118.80  E-value: 2.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIR---KTSARVAVKKIRCHAPEN-VELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkmshg 87
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKggdGKTVDVAVKTLKEDASESeRKDFLKEARVMKKLG--HPNVVRLLGVCTEEE--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTN----------TSFMLQLSSALAFLHK 157
Cdd:cd00192   70 ---PLYL-----------------------VMEYMEGGDLLDFLRKSRPVFPSPepstlslkdlLSFAIQIAKGMEYLAS 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASG---QNPEEPVSVnkcflstacgtdFYMAPEVW-EGH 233
Cdd:cd00192  124 KKFVHRDLAARNCLVGEDL--------VVKISDFGLSRDIYDDDyyrKKTGGKLPI------------RWMAPESLkDGI 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 YTAKADIFALGIIIWamlERITF-------IDTEtkkELLgSYVKQGteivpvgeALLENPkmellipvkkKSMNGRMKQ 306
Cdd:cd00192  184 FTSKSDVWSFGVLLW---EIFTLgatpypgLSNE---EVL-EYLRKG--------YRLPKP----------ENCPDELYE 238
                        330       340
                 ....*....|....*....|...
gi 119628251 307 LIKEMLAANPQDRPDAFELELRL 329
Cdd:cd00192  239 LMLSCWQLDPEDRPTFSELVERL 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
7-250 2.37e-30

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 115.95  E-value: 2.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR---CHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGMVqk 83
Cdd:cd14073    2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKkdkIEDEQDMVRIRREIEIMSSL--NHPHIIRIYEVFENKDKIV-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRK--PNRKTNtSFMLQLSSALAFLHKNQII 161
Cdd:cd14073   78 ---------------------------------IVMEYASGGELYDYISERRrlPEREAR-RIFRQIVSAVHYCHKNGVV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEGH--YTAKAD 239
Cdd:cd14073  124 HRDLKLENILLDQ--------NGNAKIADFGLSNLYS------------KDKLLQTFCGSPLYASPEIVNGTpyQGPEVD 183
                        250
                 ....*....|.
gi 119628251 240 IFALGIIIWAM 250
Cdd:cd14073  184 CWSLGVLLYTL 194
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
7-324 5.22e-30

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 115.27  E-value: 5.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH----APENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvq 82
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRkvagNDKNLQLFQREINILKSL--EHPGIVRLID---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQII 161
Cdd:cd14098   69 -----------------------WYEDDQHIYL--VMEYVEGGDLMDFIMAWGAIPEQHARELTkQILEAMAYTHSMGIT 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsDLEPTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEV-------WEGHY 234
Cdd:cd14098  124 HRDLKPENILITQ------DDPVIVKISDFGLAKVIH------------TGTFLVTFCGTMAYLAPEIlmskeqnLQGGY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 TAKADIFALGIIIWAMLER-ITFidTETKKELLGSYVKQGTEIVPvgeallenPKMELLIpvkkkSMNGRmkQLIKEMLA 313
Cdd:cd14098  186 SNLVDMWSVGCLVYVMLTGaLPF--DGSSQLPVEKRIRKGRYTQP--------PLVDFNI-----SEEAI--DFILRLLD 248
                        330
                 ....*....|.
gi 119628251 314 ANPQDRPDAFE 324
Cdd:cd14098  249 VDPEKRMTAAQ 259
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
10-248 9.75e-30

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 114.13  E-value: 9.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   10 LIREVGRGSYGVVYEAVIR----KTSARVAVKKIRCHAPENvelALREFWALSSI--KSQHPNVIHLEECILQKDgmvqk 83
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKgegeNTKIKVAVKTLKEGADEE---EREDFLEEASImkKLDHPNIVKLLGVCTQGE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   84 mshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQII 161
Cdd:pfam07714  75 ------------------------------PLYIVTEYMPGGDLLDFLRKHKRKLTLKDllSMALQIAKGMEYLESKNFV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  162 HRDLKPDNILISQTRldtsdlepTLKVADFGLSKVcsasGQNPEEPVSVNKCFLSTacgtdFYMAPEVW-EGHYTAKADI 240
Cdd:pfam07714 125 HRDLAARNCLVSENL--------VVKISDFGLSRD----IYDDDYYRKRGGGKLPI-----KWMAPESLkDGKFTSKSDV 187

                  ....*...
gi 119628251  241 FALGIIIW 248
Cdd:pfam07714 188 WSFGVLLW 195
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
6-325 1.18e-29

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 114.41  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH-----------APENVElalREFWALSSIKsqHPNVIHLEEci 74
Cdd:cd14084    6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRkftigsrreinKPRNIE---TEIEILKKLS--HPCIIKIED-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  75 lqkdgmvqkmshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALA 153
Cdd:cd14084   79 -------------------------------FFDAEDDYYI--VLELMEGGELFDRVVSNKRLKEAICKLYFyQMLLAVK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 154 FLHKNQIIHRDLKPDNILISqtrldTSDLEPTLKVADFGLSKvcsasgqnpeepVSVNKCFLSTACGTDFYMAPEVW--E 231
Cdd:cd14084  126 YLHSNGIIHRDLKPENVLLS-----SQEEECLIKITDFGLSK------------ILGETSLMKTLCGTPTYLAPEVLrsF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 232 GH--YTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIvpvgeallenpkmelLIPVKKKSMNGRMKQLIK 309
Cdd:cd14084  189 GTegYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSGKYT---------------FIPKAWKNVSEEAKDLVK 253
                        330
                 ....*....|....*.
gi 119628251 310 EMLAANPQDRPDAFEL 325
Cdd:cd14084  254 KMLVVDPSRRPSIEEA 269
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
7-325 1.25e-29

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 113.84  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRChAPENVELALREFWALSSikSQHPNVIHLEECILQKDgmvqkmsh 86
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRL-RKQNKELIINEILIMKE--CKHPNIVDYYDSYLVGD-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEyLLSRKPNRKTNT---SFMLQLSSALAFLHKNQIIHR 163
Cdd:cd06614   70 ---------------------------ELWVVMEYMDGGSLTD-IITQNPVRMNESqiaYVCREVLQGLEYLHSQNVIHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPeepvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd06614  122 DIKSDNILLSK--------DGSVKLADFGFAAQLTKEKSKR-----------NSVVGTPYWMAPEVIKRKdYGPKVDIWS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLEritfidtetkkellgsyvkqgteivpvGE-ALLENPKMELL-------IPV--KKKSMNGRMKQLIKEML 312
Cdd:cd06614  183 LGIMCIEMAE---------------------------GEpPYLEEPPLRALflittkgIPPlkNPEKWSPEFKDFLNKCL 235
                        330
                 ....*....|...
gi 119628251 313 AANPQDRPDAFEL 325
Cdd:cd06614  236 VKDPEKRPSAEEL 248
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
14-326 1.67e-29

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 113.94  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVyEAVIRKTSA---RVAVKKIRCHAPENVEL-----ALREFWALSSIksQHPNVIHLEECILqkdgmvqkms 85
Cdd:cd13994    1 IGKGATSVV-RIVTKKNPRsgvLYAVKEYRRRDDESKRKdyvkrLTSEYIISSKL--HHPNIVKVLDLCQ---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetSLKGEIafdprsayylWFVMDFCDGGDMNEYL-LSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd13994   68 --------------DLHGKW----------CLVMEYCPGGDLFTLIeKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILIsqtrldtsDLEPTLKVADFGLSkVCSASGQNPEEPVSvnkcflSTACGTDFYMAPEVW-EGHYTAKA-DIFA 242
Cdd:cd13994  124 LKPENILL--------DEDGVLKLTDFGTA-EVFGMPAEKESPMS------AGLCGSEPYMAPEVFtSGSYDGRAvDVWS 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAM-LERITFIDTETKKELLGSYVKQGTEIVpvgealLENPKMELLIPVkkksmngRMKQLIKEMLAANPQDRP- 320
Cdd:cd13994  189 CGIVLFALfTGRFPWRSAKKSDSAYKAYEKSGDFTN------GPYEPIENLLPS-------ECRRLIYRMLHPDPEKRIt 255

                 ....*...
gi 119628251 321 --DAFELE 326
Cdd:cd13994  256 idEALNDP 263
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
7-325 2.57e-29

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 113.95  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR-CHAPENV-ELALREFWALSSIKsqHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd07833    2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKeSEDDEDVkKTALREVKVLRQLR--HENIVNLKE------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNeyLLSRKPN---RKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd07833   68 ---------------------AFRRKGRLYL--VFEYVERTLLE--LLEASPGglpPDAVRSYIWQLLQAIAYCHSHNII 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASGQNPeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKAD 239
Cdd:cd07833  123 HRDIKPENILVSESG--------VLKLCDFGFARALTARPASP----------LTDYVATRWYRAPELLVGdtNYGKPVD 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLE-RITFIDTETKKEL------LGSYVKQGTEIV---PV--GEALLENPKMELLIPVKKKSMNGRMKQL 307
Cdd:cd07833  185 VWAIGCIMAELLDgEPLFPGDSDIDQLyliqkcLGPLPPSHQELFssnPRfaGVAFPEPSQPESLERRYPGKVSSPALDF 264
                        330
                 ....*....|....*...
gi 119628251 308 IKEMLAANPQDRPDAFEL 325
Cdd:cd07833  265 LKACLRMDPKERLTCDEL 282
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
8-324 2.93e-29

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 113.91  E-value: 2.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN-VELA-LREFWALSSIKSQ-HPNVIHLEEcilqkdgmvqkM 84
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgIPLStIREIALLKQLESFeHPNVVRLLD-----------V 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLQLvetslkgeiafdprsayYLwfVMDFCDGgDMNEYLlSRKPNR----KTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd07838   70 CHGPRTDRELKL-----------------TL--VFEHVDQ-DLATYL-DKCPKPglppETIKDLMRQLLRGLDFLHSHRI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSAsgQNPEEPVSVnkcflstacgTDFYMAPEVW-EGHYTAKAD 239
Cdd:cd07838  129 VHRDLKPQNILVTSDG--------QVKLADFGLARIYSF--EMALTSVVV----------TLWYRAPEVLlQSSYATPVD 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERITFIDTETKKELLGsyvkqgtEI-----VPVGEallENPKMELL----------IPVKK--KSMNG 302
Cdd:cd07838  189 MWSVGCIFAELFNRRPLFRGSSEADQLG-------KIfdvigLPSEE---EWPRNSALprssfpsytpRPFKSfvPEIDE 258
                        330       340
                 ....*....|....*....|..
gi 119628251 303 RMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd07838  259 EGLDLLKKMLTFNPHKRISAFE 280
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
8-251 3.15e-29

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 113.46  E-value: 3.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALREFWALSsiKSQHPNVIHLEeCILQkdgmvqkm 84
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldKRHIIKEKKVKYVTIEKEVLS--RLAHPGIVKLY-YTFQ-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgSNSSLYlqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05581   72 ---DESKLY-----------------------FVLEYAPNGDLLEYIRKYGSlDEKCTRFYTAEIVLALEYLHSKGIIHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsDLEptLKVADFGLSKVCSAS------GQNPEEPVSVNKCFLSTACGTDFYMAPEVW-EGHYTA 236
Cdd:cd05581  126 DLKPENILLDE------DMH--IKITDFGTAKVLGPDsspestKGDADSQIAYNQARAASFVGTAEYVSPELLnEKPAGK 197
                        250
                 ....*....|....*
gi 119628251 237 KADIFALGIIIWAML 251
Cdd:cd05581  198 SSDLWALGCIIYQML 212
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
8-251 6.02e-29

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 112.42  E-value: 6.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKSqHPNVIHLEecilqkdGMVqkmsh 86
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMkRAPGDCPENIKKEVCIQKMLS-HKNVVRFY-------GHR----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdpRSAYYLWFVMDFCDGGD----------MNEYLLSRkpnrktntsFMLQLSSALAFLH 156
Cdd:cd14069   70 -----------------------REGEFQYLFLEYASGGElfdkiepdvgMPEDVAQF---------YFQQLMAGLKYLH 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILisqtrLDTSDlepTLKVADFGLSKVCSASGQNPEepvsvnkcfLSTACGTDFYMAPEVW--EGHY 234
Cdd:cd14069  118 SCGITHRDIKPENLL-----LDEND---NLKISDFGLATVFRYKGKERL---------LNKMCGTLPYVAPELLakKKYR 180
                        250
                 ....*....|....*..
gi 119628251 235 TAKADIFALGIIIWAML 251
Cdd:cd14069  181 AEPVDVWSCGIVLFAML 197
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
14-251 7.52e-29

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 111.84  E-value: 7.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYeAVIRKTSARV-AVKKIR---CHAPENVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkmshgsn 89
Cdd:cd05123    1 LGKGSFGKVL-LVRKKDTGKLyAMKVLRkkeIIKRKEVEHTLNERNILERVN--HPFIVKL------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 ssLYlqlvetslkgeiAFDprSAYYLWFVMDFCDGGDMNeYLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd05123   59 --HY------------AFQ--TEEKLYLVLDYVPGGELF-SHLSKEGRFPEERArfYAAEIVLALEYLHSLGIIYRDLKP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQnpeepvsvnKCflSTACGTDFYMAPEVWEGH-YTAKADIFALGII 246
Cdd:cd05123  122 ENILL--------DSDGHIKLTDFGLAKELSSDGD---------RT--YTFCGTPEYLAPEVLLGKgYGKAVDWWSLGVL 182

                 ....*
gi 119628251 247 IWAML 251
Cdd:cd05123  183 LYEML 187
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
14-321 9.36e-29

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 111.69  E-value: 9.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRK-TSARVAVKkirCHAPENVElalrefwalssiKSQhpNVIHLEECILQKdgmvqkMSHGSNSSL 92
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIK---CITKKNLS------------KSQ--NLLGKEIKILKE------LSHENVVAL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 YlQLVETSlkgeiafdprSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd14120   58 L-DCQETS----------SSVYL--VMEYCNGGDLADYLQAKGTlSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNIL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 ISQT-RLDTSDLEPTLKVADFGLSKvcsasgqnpeepvsvnkcFL------STACGTDFYMAPEVWEG-HYTAKADIFAL 243
Cdd:cd14120  125 LSHNsGRKPSPNDIRLKIADFGFAR------------------FLqdgmmaATLCGSPMYMAPEVIMSlQYDAKADLWSI 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 244 GIIIWAMLERITFIDTETKKELLGSYVKQGTeivpvgeallenpkmelLIPVKKKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd14120  187 GTIVYQCLTGKAPFQAQTPQELKAFYEKNAN-----------------LRPNIPSGTSPALKDLLLGLLKRNPKDRID 247
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
7-245 1.02e-28

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 111.63  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkmsH 86
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECR--HPNIVAY---------------F 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSnsslYLQLvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM----LQlssALAFLHKNQIIH 162
Cdd:cd06613   64 GS----YLRR----------------DKLWIVMEYCGGGSLQDIYQVTGPLSELQIAYVcretLK---GLAYLHSTGKIH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldTSDLEptLKVADFGLSKVCSASgqnpeepVSVNKCFLstacGTDFYMAPEVW----EGHYTAKA 238
Cdd:cd06613  121 RDIKGANILL------TEDGD--VKLADFGVSAQLTAT-------IAKRKSFI----GTPYWMAPEVAaverKGGYDGKC 181

                 ....*..
gi 119628251 239 DIFALGI 245
Cdd:cd06613  182 DIWALGI 188
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
7-333 1.15e-28

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 111.66  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIkSQHPNVihleecilqkdgmVQKMSH 86
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRL-CGHPNI-------------VQYYDS 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLQLVetslkgeiafdprsayylWFVMDFCdGGDMNEYLLSRKPNR---KTNTSFMLQLSSALAFLHKNQ--II 161
Cdd:cd13985   67 AILSSEGRKEV------------------LLLMEYC-PGSLVDILEKSPPSPlseEEVLRIFYQICQAVGHLHSQSppII 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRldtsdlepTLKVADFGlskvcSASGQNPeepvsvnkcFLSTACG------------TDFYMAPEV 229
Cdd:cd13985  128 HRDIKIENILFSNTG--------RFKLCDFG-----SATTEHY---------PLERAEEvniieeeiqkntTPMYRAPEM 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 230 WEGH----YTAKADIFALGIIIWAMLERITFIDTETKkellgsyvkqgTEIVPVGEALLENPKMELLIpvkkksmngrmK 305
Cdd:cd13985  186 IDLYskkpIGEKADIWALGCLLYKLCFFKLPFDESSK-----------LAIVAGKYSIPEQPRYSPEL-----------H 243
                        330       340
                 ....*....|....*....|....*...
gi 119628251 306 QLIKEMLAANPQDRPDAFELELRLVQIA 333
Cdd:cd13985  244 DLIRHMLTPDPAERPDIFQVINIITKDT 271
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7-251 1.65e-28

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 110.96  E-value: 1.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELAL-REFWALSSIKsqHPNVIHLEECIlqkdgmvqk 83
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEqvAREGMVEQIkREIAIMKLLR--HPNIVELHEVM--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshGSNSSLYlqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIH 162
Cdd:cd14663   70 ---ATKTKIF-----------------------FVMELVTGGELFSKIAKNGRLKEDKARKYFqQLIDAVDYCHSRGVFH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILisqtrLDTSDlepTLKVADFGLSKVCSASGQNPeepvsvnkcFLSTACGTDFYMAPEVWE--GHYTAKADI 240
Cdd:cd14663  124 RDLKPENLL-----LDEDG---NLKISDFGLSALSEQFRQDG---------LLHTTCGTPNYVAPEVLArrGYDGAKADI 186
                        250
                 ....*....|.
gi 119628251 241 FALGIIIWAML 251
Cdd:cd14663  187 WSCGVILFVLL 197
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
7-325 1.77e-28

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 110.72  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALREFWALSSIKS--QHPNVIHLEECilqkdgmvqkm 84
Cdd:cd14099    2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVP-KSSLTKPKQREKLKSEIKIHRslKHPNIVKFHDC----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQIIHR 163
Cdd:cd14099   70 ----------------------FEDEENVYI--LLELCSNGSLMELLKRRKALTEPEVRyFMRQILSGVKYLHSNRIIHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldTSDLEptLKVADFGLSKVCsasgQNPEEpvsvNKcflSTACGTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd14099  126 DLKLGNLFL------DENMN--VKIGDFGLAARL----EYDGE----RK---KTLCGTPNYIAPEVLEKkkGHSFEVDIW 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLgSYVKQGTEIVPvgeallenpkmellipvKKKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd14099  187 SLGVILYTLLVGKPPFETSDVKETY-KRIKKNEYSFP-----------------SHLSISDEAKDLIRSMLQPDPTKRPS 248

                 ....
gi 119628251 322 AFEL 325
Cdd:cd14099  249 LDEI 252
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
15-251 2.30e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 110.46  E-value: 2.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAvIRKTSAR--VAVK-----KIRCHAPENVelaLREFWALSSIKsqHPNVIHLEEciLQKDgmvqkmshg 87
Cdd:cd14121    4 GSGTYATVYKA-YRKSGARevVAVKcvsksSLNKASTENL---LTEIELLKKLK--HPHIVELKD--FQWD--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsAYYLWFVMDFCDGGDMNEYLLSRK--PNRkTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd14121   67 ------------------------EEHIYLIMEYCSGGDLSRFIRSRRtlPES-TVRRFLQQLASALQFLREHNISHMDL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILIsqtrldTSDLEPTLKVADFGLSKVCSasgqNPEEPVSVNkcflstacGTDFYMAPE-VWEGHYTAKADIFALG 244
Cdd:cd14121  122 KPQNLLL------SSRYNPVLKLADFGFAQHLK----PNDEAHSLR--------GSPLYMAPEmILKKKYDARVDLWSVG 183

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd14121  184 VILYECL 190
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
9-325 4.53e-28

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 109.99  E-value: 4.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   9 DLIREVGRGSYGVVYEAVIRKTSARVAVKKIrcHAPENVE---LALREFWALssIKSQHPNVIhleECilqkdgmvqkms 85
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKI--HVDGDEEfrkQLLRELKTL--RSCESPYVV---KC------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLH-KNQIIHR 163
Cdd:cd06623   65 YG------------------AFYKEGEISI--VLEYMDGGSLADLLKKVGKIPEPVLAYIArQILKGLDYLHtKRHIIHR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldtSDLEPtlKVADFGLSKVCSASGQNpeepvsvnkCflSTACGTDFYMAPEVWEG-HYTAKADIFA 242
Cdd:cd06623  125 DIKPSNLLIN------SKGEV--KIADFGISKVLENTLDQ---------C--NTFVGTVTYMSPERIQGeSYSYAADIWS 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMleritfidtetkkeLLGSY----VKQGTEIvpvgeALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQD 318
Cdd:cd06623  186 LGLTLLEC--------------ALGKFpflpPGQPSFF-----ELMQAICDGPPPSLPAEEFSPEFRDFISACLQKDPKK 246

                 ....*..
gi 119628251 319 RPDAFEL 325
Cdd:cd06623  247 RPSAAEL 253
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-325 4.64e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 110.35  E-value: 4.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchAPENV---ELALREFWALSsiKSQHPNVIHLEECILQK--DGMVQ 82
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIR--LPNNElarEKVLREVRALA--KLDHPGIVRYFNAWLERppEGWQE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMShgsnsslylqlvetslkgeiafdprsAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML----QLSSALAFLHKN 158
Cdd:cd14048   84 KMD--------------------------EVYLYIQMQLCRKENLKDWMNRRCTMESRELFVCLnifkQIASAVEYLHSK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISqtrldtsdLEPTLKVADFGLSkvcSASGQNPEEpVSVNKCFLSTA-----CGTDFYMAPEVWEGH 233
Cdd:cd14048  138 GLIHRDLKPSNVFFS--------LDDVVKVGDFGLV---TAMDQGEPE-QTVLTPMPAYAkhtgqVGTRLYMSPEQIHGN 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 -YTAKADIFALGIIIWamleritfidtetkkELLGSYVKQGTEIVPVGEAllenpkMELLIPVKKKSMNGRMKQLIKEML 312
Cdd:cd14048  206 qYSEKVDIFALGLILF---------------ELIYSFSTQMERIRTLTDV------RKLKFPALFTNKYPEERDMVQQML 264
                        330
                 ....*....|...
gi 119628251 313 AANPQDRPDAFEL 325
Cdd:cd14048  265 SPSPSERPEAHEV 277
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-329 6.57e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 109.50  E-value: 6.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEnvelALREFWALSSIksQHPNVIHLEECILQKDGMVQKMShg 87
Cdd:cd14047    8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK----AEREVKALAKL--DHPNIVRYNGCWDGFDYDPETSS-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLylqlVETSlkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRkpNRKTNTSFM-----LQLSSALAFLHKNQIIH 162
Cdd:cd14047   80 SNSSR----SKTK-------------CLFIQMEFCEKGTLESWIEKR--NGEKLDKVLaleifEQITKGVEYIHSKKLIH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsdlepTLKVADFGLskVCSASGQNPeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd14047  141 RDLKPSNIFLVDTG--------KVKIGDFGL--VTSLKNDGK----------RTKSKGTLSYMSPEQISSQdYGKEVDIY 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLEriTFIDTETKKELLGSyVKQGteIVPVGeaLLENPKMEllipvkkksmngrmKQLIKEMLAANPQDRPD 321
Cdd:cd14047  201 ALGLILFELLH--VCDSAFEKSKFWTD-LRNG--ILPDI--FDKRYKIE--------------KTIIKKMLSKKPEDRPN 259

                 ....*...
gi 119628251 322 AFELELRL 329
Cdd:cd14047  260 ASEILRTL 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
14-250 1.22e-27

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 109.10  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN-VELALREFWALSSIK-SQHPNVIHLEECILQkdgmvqkmshgsnss 91
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDdVSDIQKEVALLSQLKlGQPKNIIKYYGSYLK--------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafDPRsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd06917   74 ----------------GPS----LWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANIL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 ISQTRldtsdlepTLKVADFGL-SKVCSASGQNpeepvsvnkcflSTACGTDFYMAPEV-WEG-HYTAKADIFALGIIIW 248
Cdd:cd06917  134 VTNTG--------NVKLCDFGVaASLNQNSSKR------------STFVGTPYWMAPEViTEGkYYDTKADIWSLGITTY 193

                 ..
gi 119628251 249 AM 250
Cdd:cd06917  194 EM 195
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
7-322 1.50e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 110.34  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrCHAPENVELA---LREFWALSSIKsQHPNVIHLEECILQKdgmvqk 83
Cdd:cd07852    8 RYEILKKLGKGAYGIVWKAIDKKTGEVVALKKI-FDAFRNATDAqrtFREIMFLQELN-DHPNIIKLLNVIRAE------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgSNSSLYL--QLVETSL----KGEIAFDPRSAYYLWfvmdfcdggdmneyllsrkpnrktntsfmlQLSSALAFLHK 157
Cdd:cd07852   80 ----NDKDIYLvfEYMETDLhaviRANILEDIHKQYIMY------------------------------QLLKALKYLHS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNPEEPVsvnkcfLSTACGTDFYMAPEVWEG--HYT 235
Cdd:cd07852  126 GGVIHRDLKPSNILL--------NSDCRVKLADFGLARSLSQLEEDDENPV------LTDYVATRWYRAPEILLGstRYT 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAM---------------LERI-TFIDTETKKEL--LGSyvkqgteivPVGEALLENpkmelLIPVKK 297
Cdd:cd07852  192 KGVDMWSVGCILGEMllgkplfpgtstlnqLEKIiEVIGRPSAEDIesIQS---------PFAATMLES-----LPPSRP 257
                        330       340       350
                 ....*....|....*....|....*....|..
gi 119628251 298 KSMNGRMKQ-------LIKEMLAANPQDRPDA 322
Cdd:cd07852  258 KSLDELFPKaspdaldLLKKLLVFNPNKRLTA 289
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
7-321 1.55e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 108.56  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIRE--VGRGSYGVVYEAVIR-KTSARVAVKKI-RCHAPENVELALREFWALSSIKsqHPNVIHLEEcilqkdgmVQ 82
Cdd:cd14202    1 KFEFSRKdlIGHGAFAVVFKGRHKeKHDLEVAVKCInKKNLAKSQTLLGKEIKILKELK--HENIVALYD--------FQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMShgsnSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLS-RKPNRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd14202   71 EIA----NSVYL-----------------------VMEYCNGGDLADYLHTmRTLSEDTIRLFLQQIAGAMKMLHSKGII 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRLDTSDlePT---LKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEV-WEGHYTAK 237
Cdd:cd14202  124 HRDLKPQNILLSYSGGRKSN--PNnirIKIADFGFARYLQ------------NNMMAATLCGSPMYMAPEViMSQHYDAK 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTeivpvgeallenpkmelLIPVKKKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd14202  190 ADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKS-----------------LSPNIPRETSSHLRQLLLGLLQRNQK 252

                 ....
gi 119628251 318 DRPD 321
Cdd:cd14202  253 DRMD 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
15-251 2.17e-27

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 107.74  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYeAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkmshgsnsslyl 94
Cdd:cd14006    2 GRGRFGVVK-RCIEKATGREFAAKFIPKRDKKKEAVLREISILNQL--QHPRIIQLHE---------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  95 qlvetslkgeiAFDPRsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTN-TSFMLQLSSALAFLHKNQIIHRDLKPDNILIS 173
Cdd:cd14006   57 -----------AYESP--TELVLILELCSGGELLDRLAERGSLSEEEvRTYMRQLLEGLQYLHNHHILHLDLKPENILLA 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 174 QTRldtsdlEPTLKVADFGLskvcsASGQNPEEPVSVNkcflstaCGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd14006  124 DRP------SPQIKIIDFGL-----ARKLNPGEELKEI-------FGTPEFVAPEIVNGEpVSLATDMWSIGVLTYVLL 184
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
8-319 3.48e-27

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 107.34  E-value: 3.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVELAL-REFWALSSIksQHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVnkEKLSKESVLMKVeREIAIMKLI--EHPNVLKLYDVY---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgSNSSlylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14081   71 ---ENKK----------------------YLYLVLEYVSGGELFDYLVKKGRlTEKEARKFFRQIISALDYCHSHSICHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCsasgqnpeepvsVNKCFLSTACGTDFYMAPEVWEG-HYT-AKADIF 241
Cdd:cd14081  126 DLKPENLLL--------DEKNNIKIADFGMASLQ------------PEGSLLETSCGSPHYACPEVIKGeKYDgRKADIW 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLGSyVKQGTEIVPVgeallenpkmelLIPVKKKSmngrmkqLIKEMLAANPQDR 319
Cdd:cd14081  186 SCGVILYALLVGALPFDDDNLRQLLEK-VKRGVFHIPH------------FISPDAQD-------LLRRMLEVNPEKR 243
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
8-320 4.45e-27

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 107.09  E-value: 4.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEaVIRKTSARV-AVKKI--RCHAPENVELALREFWALSSIKsqHPNVIHLEECILqkdgmvqkm 84
Cdd:cd08530    2 FKVLKKLGKGSYGSVYK-VKRLSDNQVyALKEVnlGSLSQKEREDSVNEIRLLASVN--HPNIIRYKEAFL--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafDPRSayyLWFVMDFCDGGDMNEYLLSRKPNRKTNT-----SFMLQLSSALAFLHKNQ 159
Cdd:cd08530   70 -----------------------DGNR---LCIVMEYAPFGDLSKLISKRKKKRRLFPeddiwRIFIQMLRGLKALHDQK 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVcsasgqnpeepvsVNKCFLSTACGTDFYMAPEVWEGH-YTAKA 238
Cdd:cd08530  124 ILHRDLKSANILLSAGDL--------VKIGDLGISKV-------------LKKNLAKTQIGTPLYAAPEVWKGRpYDYKS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAMLERITFIDTETKKELlgSYVKQGTEIVPvgeallenpkmellIPvkkKSMNGRMKQLIKEMLAANPQD 318
Cdd:cd08530  183 DIWSLGCLLYEMATFRPPFEARTMQEL--RYKVCRGKFPP--------------IP---PVYSQDLQQIIRSLLQVNPKK 243

                 ..
gi 119628251 319 RP 320
Cdd:cd08530  244 RP 245
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
7-252 5.64e-27

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 106.93  E-value: 5.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkm 84
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEkiPKSDLKSVMGEIDLLKKLN--HPNIVKYIGSVKTKD------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDmneyLLSR-KPNRKTNTS----FMLQLSSALAFLHKNQ 159
Cdd:cd06627   73 -----------------------------SLYIILEYVENGS----LASIiKKFGKFPESlvavYIYQVLEGLAYLHEQG 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPEVWEGH-YTAKA 238
Cdd:cd06627  120 VIHRDIKGANILTTKDGL--------VKLADFGVATKLNEVEKDENSVV-----------GTPYWMAPEVIEMSgVTTAS 180
                        250
                 ....*....|....
gi 119628251 239 DIFALGIIIWAMLE 252
Cdd:cd06627  181 DIWSVGCTVIELLT 194
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
8-251 7.06e-27

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 107.33  E-value: 7.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRefwalssiKSQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKiidKSKRDPSEEIEILLR--------YGQHPNIITLRD------------ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRK--PNRKTnTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd14091   62 ---------------------VYDDGNSVYL--VTELLRGGELLDRILRQKffSEREA-SAVMKTLTKTVEYLHSQGVVH 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISqtrlDTSDLEPTLKVADFGLSKVCSAS-GqnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADI 240
Cdd:cd14091  118 RDLKPSNILYA----DESGDPESLRICDFGFAKQLRAEnG------------LLMTPCYTANFVAPEVLKKQgYDAACDI 181
                        250
                 ....*....|.
gi 119628251 241 FALGIIIWAML 251
Cdd:cd14091  182 WSLGVLLYTML 192
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
7-322 1.59e-26

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 107.23  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELA---LREFWALSSIKsqHPNVIHLEECILQKDGMvqk 83
Cdd:cd07834    1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS-NVFDDLIDAkriLREIKILRHLK--HENIIGLLDILRPPSPE--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEYLLSRKPnrktnTS------FMLQLSSALAFLHK 157
Cdd:cd07834   75 ----EFNDVYI-----------------------VTELMET-DLHKVIKSPQP-----LTddhiqyFLYQILRGLKYLHS 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISqtrldtSDLEptLKVADFGLskvcsASGQNPEEpvsvNKCFLSTACGTDFYMAPEV---WEgHY 234
Cdd:cd07834  122 AGVIHRDLKPSNILVN------SNCD--LKICDFGL-----ARGVDPDE----DKGFLTEYVVTRWYRAPELllsSK-KY 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 TAKADIFALGIIIWAMLERitfidtetkKELLG--SYVKQGTEIV-----PVGEAL--LENPK----MELLIPVKKKSMN 301
Cdd:cd07834  184 TKAIDIWSVGCIFAELLTR---------KPLFPgrDYIDQLNLIVevlgtPSEEDLkfISSEKarnyLKSLPKKPKKPLS 254
                        330       340
                 ....*....|....*....|....*...
gi 119628251 302 GRMKQ-------LIKEMLAANPQDRPDA 322
Cdd:cd07834  255 EVFPGaspeaidLLEKMLVFNPKKRITA 282
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
7-245 2.26e-26

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 105.46  E-value: 2.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELA-----LREFwalssikSQHPNVIHLEECILQKDgmv 81
Cdd:cd06608    7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKleiniLRKF-------SNHPNIATFYGAFIKKD--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafDPRSAYYLWFVMDFCDGGDMNEYL--LSRKPNRKTN---TSFMLQLSSALAFLH 156
Cdd:cd06608   77 --------------------------PPGGDDQLWLVMEYCGGGSVTDLVkgLRKKGKRLKEewiAYILRETLRGLAYLH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILIsqtrldTSDLEptLKVADFGLS-KVCSASGQNpeepvsvnkcflSTACGTDFYMAPEV------ 229
Cdd:cd06608  131 ENKVIHRDIKGQNILL------TEEAE--VKLVDFGVSaQLDSTLGRR------------NTFIGTPYWMAPEViacdqq 190
                        250
                 ....*....|....*.
gi 119628251 230 WEGHYTAKADIFALGI 245
Cdd:cd06608  191 PDASYDARCDVWSLGI 206
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
13-327 2.42e-26

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 105.16  E-value: 2.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRktSARVAVKKIRCHApeNVELALREFWA-LSSIKSQHPNVIHLeecilqkdgmvqkmshgsnss 91
Cdd:cd13979   10 PLGSGGFGSVYKATYK--GETVAVKIVRRRR--KNRASRQSFWAeLNAARLRHENIVRV--------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetsLKGEIAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP----NRKTNtsFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd13979   65 ---------LAAETGTDFASLGLI--IMEYCGNGTLQQLIYEGSEplplAHRIL--ISLDIARALRFCHSHGIVHLDVKP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISqtrldtsdLEPTLKVADFGLSKVCSAsGQNPEEPVSVNKcflstacGTDFYMAPEVWEGH-YTAKADIFALGII 246
Cdd:cd13979  132 ANILIS--------EQGVCKLCDFGCSVKLGE-GNEVGTPRSHIG-------GTYTYRAPELLKGErVTPKADIYSFGIT 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 247 IWAMLERITFIDTEtkkellgsyvKQGTEIVPVGEALleNPKMElliPVKKKSMNGRMKQLIKEMLAANPQDRPDAFELE 326
Cdd:cd13979  196 LWQMLTRELPYAGL----------RQHVLYAVVAKDL--RPDLS---GLEDSEFGQRLRSLISRCWSAQPAERPNADESL 260

                 .
gi 119628251 327 L 327
Cdd:cd13979  261 L 261
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
15-319 2.97e-26

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 106.14  E-value: 2.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALREFWALSsIKSQHPNVIHLEECIlqkdgmvQKMSHgsnss 91
Cdd:cd05570    4 GKGSFGKVMLAERKKTDELYAIKvlkKEVIIEDDDVECTMTEKRVLA-LANRHPFLTGLHACF-------QTEDR----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafdprsayyLWFVMDFCDGGD-MNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd05570   71 -----------------------LYFVMEYVNGGDlMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNV 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSvNKCFLSTACGTDFYMAPE-VWEGHYTAKADIFALGIIIWA 249
Cdd:cd05570  128 LL--------DAEGHIKIADFGMCK----------EGIW-GGNTTSTFCGTPDYIAPEiLREQDYGFSVDWWALGVLLYE 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 250 MLERITFIDTETKKELLgsyvkqgteivpvgEALLENpkmELLIPVkkkSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd05570  189 MLAGQSPFEGDDEDELF--------------EAILND---EVLYPR---WLSREAVSILKGLLTKDPARR 238
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
8-322 3.12e-26

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 105.72  E-value: 3.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHApENVEL---ALREFWALSSIksQHPNVIHLEECilqkdgMVQKM 84
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN-EKEGFpitAIREIKLLQKL--DHPNVVRLKEI------VTSKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEyLLSRKPNRKTNT---SFMLQLSSALAFLHKNQII 161
Cdd:cd07840   72 SAKYKGSIYM-----------------------VFEYMDH-DLTG-LLDNPEVKFTESqikCYMKQLLEGLQYLHSNGIL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVSVnkcflstacgTDFYMAPEVWEG--HYTAKAD 239
Cdd:cd07840  127 HRDIKGSNILINN--------DGVLKLADFGLARPYTKENNADYTNRVI----------TLWYRPPELLLGatRYGPEVD 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERITFI--DTETKK-----ELLGS-------YVKQgteiVPVGEALLENPKME-LLIPVKKKSMNGRM 304
Cdd:cd07840  189 MWSVGCILAELFTGKPIFqgKTELEQlekifELCGSpteenwpGVSD----LPWFENLKPKKPYKrRLREVFKNVIDPSA 264
                        330
                 ....*....|....*...
gi 119628251 305 KQLIKEMLAANPQDRPDA 322
Cdd:cd07840  265 LDLLDKLLTLDPKKRISA 282
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
3-325 3.67e-26

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 105.28  E-value: 3.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   3 SSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrchaPENVELALREFWALSSIKsqHPNVIHLEECILqkdgmvq 82
Cdd:cd14137    1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV----LQDKRYKNRELQIMRRLK--HPNIVKLKYFFY------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmSHGSNsslylqlvetslKGEIafdprsayYLWFVMDFcdggdMNEYL--LSRKPNRKTNT-------SFMLQLSSALA 153
Cdd:cd14137   68 --SSGEK------------KDEV--------YLNLVMEY-----MPETLyrVIRHYSKNKQTipiiyvkLYSYQLFRGLA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 154 FLHKNQIIHRDLKPDNILISQtrlDTSdlepTLKVADFGlskvcSASGQNPEEPvSVnkcflSTACgTDFYMAPEVWEG- 232
Cdd:cd14137  121 YLHSLGICHRDIKPQNLLVDP---ETG----VLKLCDFG-----SAKRLVPGEP-NV-----SYIC-SRYYRAPELIFGa 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 -HYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVK-QGTeivPVGEALLE-NPK-MELLIP-VKKKSM----NGR 303
Cdd:cd14137  182 tDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKvLGT---PTREQIKAmNPNyTEFKFPqIKPHPWekvfPKR 258
                        330       340
                 ....*....|....*....|....*.
gi 119628251 304 MKQ----LIKEMLAANPQDRPDAFEL 325
Cdd:cd14137  259 TPPdaidLLSKILVYNPSKRLTALEA 284
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
7-248 7.36e-26

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 103.87  E-value: 7.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELAL--REFWALSSIKsqHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNlrQEIEILRKLN--HPNIIEMLDSF---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvETslKGEIAFdprsayylwfVMDFCDGgDMNEYL-----LSRKPNRktntSFMLQLSSALAFLHKNQ 159
Cdd:cd14002   70 -------------ET--KKEFVV----------VTEYAQG-ELFQILeddgtLPEEEVR----SIAKQLVSALHYLHSNR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVcsasgqnpeepVSVNKCFLSTACGTDFYMAPE-VWEGHYTAKA 238
Cdd:cd14002  120 IIHRDMKPQNILIGKGGV--------VKLCDFGFARA-----------MSCNTLVLTSIKGTPLYMAPElVQEQPYDHTA 180
                        250
                 ....*....|
gi 119628251 239 DIFALGIIIW 248
Cdd:cd14002  181 DLWSLGCILY 190
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
6-253 7.88e-26

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 105.53  E-value: 7.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrCHAPENVELA---LREFWALSSIKsqHPNVIHLEECILQKdgmvQ 82
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKI-PNAFDVVTTAkrtLRELKILRHFK--HDNIIAIRDILRPK----V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVETSLKGEIafdprsayylwfvmdFCDGGDMNEYLlsrkpnrktnTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd07855   78 PYADFKDVYVVLDLMESDLHHII---------------HSDQPLTLEHI----------RYFLYQLLRGLKYIHSANVIH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSasgQNPEEpvsvNKCFLSTACGTDFYMAPEVW--EGHYTAKADI 240
Cdd:cd07855  133 RDLKPSNLLVNE--------NCELKIGDFGMARGLC---TSPEE----HKYFMTEYVATRWYRAPELMlsLPEYTQAIDM 197
                        250
                 ....*....|...
gi 119628251 241 FALGIIIWAMLER 253
Cdd:cd07855  198 WSVGCIFAEMLGR 210
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
15-251 7.90e-26

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 103.79  E-value: 7.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVK----KIRCHAPENVELALREFWALSSI--------KSQHPNVIHLEECIlqKDGMVQ 82
Cdd:cd14008    2 GRGSFGKVKLALDTETGQLYAIKifnkSRLRKRREGKNDRGKIKNALDDVrreiaimkKLDHPNIVRLYEVI--DDPESD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KmshgsnssLYLqlvetslkgeiafdprsayylwfVMDFCDGGD-MNEYLLSRKPN------RKTntsfMLQLSSALAFL 155
Cdd:cd14008   80 K--------LYL-----------------------VLEYCEGGPvMELDSGDRVPPlpeetaRKY----FRDLVLGLEYL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYT 235
Cdd:cd14008  125 HENGIVHRDIKPENLLLTADG--------TVKISDFGVSEMFEDGND-----------TLQKTAGTPAFLAPELCDGDSK 185
                        250       260
                 ....*....|....*....|
gi 119628251 236 A----KADIFALGIIIWAML 251
Cdd:cd14008  186 TysgkAADIWALGVTLYCLV 205
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
8-325 9.16e-26

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 103.65  E-value: 9.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAViRKTSARVAVKK---IRCHAPENVELALREFWALSSIKsqHPNVIHLEECILQKDgmvqkm 84
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVV-RKVDGRVYALKqidISRMSRKMREEAIDEARVLSKLN--SPYVIKYYDSFVDKG------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYL---LSRKPNRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd08529   73 -----------------------------KLNIVMEYAENGDLHSLIksqRGRPLPEDQIWKFFIQTLLGLSHLHSKKIL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADI 240
Cdd:cd08529  124 HRDIKSMNIFLDKG--------DNVKIGDLGVAKILSDTTN-----------FAQTIVGTPYYLSPELCEDKpYNEKSDV 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWamlERITF---IDTETKKELLGSYVKQGTEIVPvgeallenpkmellipvkkKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd08529  185 WALGCVLY---ELCTGkhpFEAQNQGALILKIVRGKYPPIS-------------------ASYSQDLSQLIDSCLTKDYR 242

                 ....*...
gi 119628251 318 DRPDAFEL 325
Cdd:cd08529  243 QRPDTTEL 250
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
2-253 9.55e-26

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 104.70  E-value: 9.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   2 VSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH-APENVEL-ALREFWALSSIKsqHPNVIHLEEcilqkdg 79
Cdd:cd07866    4 CSKLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHnEKDGFPItALREIKILKKLK--HPNVVPLID------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 MVqkmshgsnsslylqlVETSlkGEIAFDPRSAYYLWFVMDfcdgGDMNEYLlsRKPNRKTNTS----FMLQLSSALAFL 155
Cdd:cd07866   75 MA---------------VERP--DKSKRKRGSVYMVTPYMD----HDLSGLL--ENPSVKLTESqikcYMLQLLEGINYL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEG--H 233
Cdd:cd07866  132 HENHILHRDIKAANILIDNQ--------GILKIADFGLARPYDGPPPNPKGGGGGGTRKYTNLVVTRWYRPPELLLGerR 203
                        250       260
                 ....*....|....*....|
gi 119628251 234 YTAKADIFALGIIIWAMLER 253
Cdd:cd07866  204 YTTAVDIWGIGCVFAEMFTR 223
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
7-251 1.03e-25

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 103.95  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrcHAP---ENVEL-ALREFWALSSIKSqHPNVIHLEECILqkdgmvq 82
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKV--ALRkleGGIPNqALREIKALQACQG-HPYVVKLRDVFP------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmsHGSNSSLYLQLVETSLkgeiafdprsayylWFVMdfcdgGDmneyllSRKP-NRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd07832   71 ---HGTGFVLVFEYMLSSL--------------SEVL-----RD------EERPlTEAQVKRYMRMLLKGVAYMHANRIM 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKAD 239
Cdd:cd07832  123 HRDLKPANLLISSTGV--------LKIADFGLARLFSEEDPRL----------YSHQVATRWYRAPELLYGsrKYDEGVD 184
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd07832  185 LWAVGCIFAELL 196
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
7-322 1.85e-25

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 103.99  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRChapENVE-----LALREFWALSSIKsqHPNVIHLEECILQKdgmv 81
Cdd:cd07865   13 KYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLM---ENEKegfpiTALREIKILQLLK--HENVVNLIEICRTK---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMSHGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDgGDMNEyLLSrKPNRKTNTS----FMLQLSSALAFLHK 157
Cdd:cd07865   84 ATPYNRYKGSIYL-----------------------VFEFCE-HDLAG-LLS-NKNVKFTLSeikkVMKMLLNGLYYIHR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASgQNPEEPVSVNKCFlstacgTDFYMAPEVWEG--HYT 235
Cdd:cd07865  138 NKILHRDMKAANILITKDGV--------LKLADFGLARAFSLA-KNSQPNRYTNRVV------TLWYRPPELLLGerDYG 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAMLER--ITFIDTETKK-----ELLGSYVKqgtEIVPVGEALLENPKMELliPV-KKKSMNGRMK-- 305
Cdd:cd07865  203 PPIDMWGAGCIMAEMWTRspIMQGNTEQHQltlisQLCGSITP---EVWPGVDKLELFKKMEL--PQgQKRKVKERLKpy 277
                        330       340
                 ....*....|....*....|....
gi 119628251 306 -------QLIKEMLAANPQDRPDA 322
Cdd:cd07865  278 vkdpyalDLIDKLLVLDPAKRIDA 301
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
7-246 4.54e-25

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 103.13  E-value: 4.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAV--IRKTSARVAVKKIRCHAPENVEL---ALREFWALSSIKsqHPNVIHLEECILqkdgmv 81
Cdd:cd07842    1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEQYTGIsqsACREIALLRELK--HENVVSLVEVFL------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmsHGSNSSLYLqlvetslkgeiAFDpRSAYYLWFVMDFcdggdmneyllSRKPNRK-----TNTSFMLQLSSALAFLH 156
Cdd:cd07842   73 ----EHADKSVYL-----------LFD-YAEHDLWQIIKF-----------HRQAKRVsippsMVKSLLWQILNGIHYLH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILIsqtrldTSDLEP--TLKVADFGLSKVCSASGQNP--EEPVSVnkcflstacgTDFYMAPEVWEG 232
Cdd:cd07842  126 SNWVLHRDLKPANILV------MGEGPErgVVKIGDLGLARLFNAPLKPLadLDPVVV----------TIWYRAPELLLG 189
                        250
                 ....*....|....*.
gi 119628251 233 --HYTAKADIFALGII 246
Cdd:cd07842  190 arHYTKAIDIWAIGCI 205
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
8-325 5.47e-25

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 101.31  E-value: 5.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR--CHAPENVELALREFWALSSIKsQHPNVIHLEeCILQKDGMvqkms 85
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKkpFRGPKERARALREVEAHAALG-QHPNIVRYY-SSWEEGGH----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnssLYLQlvetslkgeiafdprsayylwfvMDFCDGGDMNEYLLSRKPNRKTNT----SFMLQLSSALAFLHKNQII 161
Cdd:cd13997   75 ------LYIQ-----------------------MELCENGSLQDALEELSPISKLSEaevwDLLLQVALGLAFIHSKGIV 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEepvsvnkcflstacGTDFYMAPEVWEGHYT--AKAD 239
Cdd:cd13997  126 HLDIKPDNIFISN--------KGTCKIGDFGLATRLETSGDVEE--------------GDSRYLAPELLNENYThlPKAD 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGiiiwamlerITFIDTETKKELlgsyvkqgteivPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd13997  184 IFSLG---------VTVYEAATGEPL------------PRNGQQWQQLRQGKLPLPPGLVLSQELTRLLKVMLDPDPTRR 242

                 ....*.
gi 119628251 320 PDAFEL 325
Cdd:cd13997  243 PTADQL 248
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
8-325 7.10e-25

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 101.58  E-value: 7.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVeLALREFWALSSIkSQHPNVIHLEECILQKdgmvqkmS 85
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMkkHFKSLEQV-NNLREIQALRRL-SPHPNILRLIEVLFDR-------K 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSnsslyLQLVetslkgeiafdprsayylwfvmdfCDGGDMNEYLLSRKPNR----KTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd07831   72 TGR-----LALV------------------------FELMDMNLYELIKGRKRplpeKRVKNYMYQLLKSLDHMHRNGIF 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTrldtsdlepTLKVADFGlsKVCSASGQNP-EEPVSvnkcflstacgTDFYMAPE--VWEGHYTAKA 238
Cdd:cd07831  123 HRDIKPENILIKDD---------ILKLADFG--SCRGIYSKPPyTEYIS-----------TRWYRAPEclLTDGYYGPKM 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAM------------LERITFI-------DTETKKELLGSYV-------KQGTEIvpvgeallenpkmELL 292
Cdd:cd07831  181 DIWAVGCVFFEIlslfplfpgtneLDQIAKIhdvlgtpDAEVLKKFRKSRHmnynfpsKKGTGL-------------RKL 247
                        330       340       350
                 ....*....|....*....|....*....|...
gi 119628251 293 IPvkkkSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd07831  248 LP----NASAEGLDLLKKLLAYDPDERITAKQA 276
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
8-253 1.03e-24

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 101.21  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENV-ELALREfwaLSSIKS-QHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLeTEDEGVpSTAIRE---ISLLKElNHPNIVRLLDVV---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 sHgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEYLLSrKPNRKTN----TSFMLQLSSALAFLHKNQI 160
Cdd:cd07835   68 -H-SENKLYL-----------------------VFEFLDL-DLKKYMDS-SPLTGLDppliKSYLYQLLQGIAFCHSHRV 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsASG----QNPEEPVsvnkcflstacgTDFYMAPEVWEG--HY 234
Cdd:cd07835  121 LHRDLKPQNLLI--------DTEGALKLADFGLAR---AFGvpvrTYTHEVV------------TLWYRAPEILLGskHY 177
                        250
                 ....*....|....*....
gi 119628251 235 TAKADIFALGIIIWAMLER 253
Cdd:cd07835  178 STPVDIWSVGCIFAEMVTR 196
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
8-319 1.29e-24

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 100.60  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALREFWALSSIKSQ--------------HPNVIHLEEC 73
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIP-RASNAGLKKEREKRLEKEISRDirtireaalssllnHPHICRLRDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQkdgmvqkmshgsnsslylqlvetslkgeiafdpRSAYYLWFvmDFCDGGDMNEYLLSRKPNR-KTNTSFMLQLSSAL 152
Cdd:cd14077   82 LRT---------------------------------PNHYYMLF--EYVDGGQLLDYIISHGKLKeKQARKFARQIASAL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 153 AFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWEG 232
Cdd:cd14077  127 DYLHRNSIVHRDLKIENILISKSG--------NIKIIDFGLSNLYDPRRL------------LRTFCGSLYFAAPELLQA 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 H-YTA-KADIFALGIIIWAML-ERITFIDTETkkELLGSYVKQGTeivpvgealLENPkmellipvkkKSMNGRMKQLIK 309
Cdd:cd14077  187 QpYTGpEVDVWSFGVVLYVLVcGKVPFDDENM--PALHAKIKKGK---------VEYP----------SYLSSECKSLIS 245
                        330
                 ....*....|
gi 119628251 310 EMLAANPQDR 319
Cdd:cd14077  246 RMLVVDPKKR 255
Pkinase pfam00069
Protein kinase domain;
8-325 1.85e-24

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 98.86  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL--ALREFWALSsiKSQHPNVIHLEECILQKDgmvqkms 85
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILK--KLNHPNIVRLYDAFEDKD------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   86 hgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAflhknqi 160
Cdd:pfam00069  72 ----------------------------NLYLVLEYVEGGSLFDLLsekgaFSEREAKF----IMKQILEGLE------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  161 ihrdlkpdnilisqtrldtsdleptlkvadfglskvcsasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEG-HYTAKAD 239
Cdd:pfam00069 113 --------------------------------------------------SGSSLTTFVGTPWYMAPEVLGGnPYGPKVD 142
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  240 IFALGIIIWAMLeritfidteTKKELLgsyvkQGTEIVPVGEALLENPKMELLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:pfam00069 143 VWSLGCILYELL---------TGKPPF-----PGINGNEIYELIIDQPYAFPELP---SNLSEEAKDLLKKLLKKDPSKR 205

                  ....*.
gi 119628251  320 PDAFEL 325
Cdd:pfam00069 206 LTATQA 211
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
8-253 2.08e-24

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 100.59  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHLEECILqkdgmvqkmshg 87
Cdd:cd06611    7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECK--HPNIVGLYEAYF------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiaFDPRsayyLWFVMDFCDGGDMNEYLLS-RKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDL 165
Cdd:cd06611   73 -------------------YENK----LWILIEFCDGGALDSIMLElERGLTEPQIRYvCRQMLEALNFLHSHKVIHRDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISqtrldtsdLEPTLKVADFGLSKVCSASGQNPeepvsvnkcflSTACGTDFYMAPEVW------EGHYTAKAD 239
Cdd:cd06611  130 KAGNILLT--------LDGDVKLADFGVSAKNKSTLQKR-----------DTFIGTPYWMAPEVVacetfkDNPYDYKAD 190
                        250
                 ....*....|....
gi 119628251 240 IFALGIIIWAMLER 253
Cdd:cd06611  191 IWSLGITLIELAQM 204
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
7-322 2.34e-24

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 100.20  E-value: 2.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENV-ELALREFWALSSIKsqHPNVIHLEECILqkdgmvqkm 84
Cdd:cd07839    1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLdDDDEGVpSSALREICLLKELK--HKNIVRLYDVLH--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEYL--LSRKPNRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd07839   70 ---SDKKLTL-----------------------VFEYCDQ-DLKKYFdsCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKvcsASGQnpeePVsvnKCFlSTACGTDFYMAPEVWEGH--YTAKADI 240
Cdd:cd07839  123 RDLKPQNLLINK--------NGELKLADFGLAR---AFGI----PV---RCY-SAEVVTLWYRPPDVLFGAklYSTSIDM 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLE--RITF----IDTETKK--ELLGSYVKQ---GTEIVPVGEALLENPKMELLIPVKKKsMNGRMKQLIK 309
Cdd:cd07839  184 WSAGCIFAELANagRPLFpgndVDDQLKRifRLLGTPTEEswpGVSKLPDYKPYPMYPATTSLVNVVPK-LNSTGRDLLQ 262
                        330
                 ....*....|...
gi 119628251 310 EMLAANPQDRPDA 322
Cdd:cd07839  263 NLLVCNPVQRISA 275
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
8-252 2.72e-24

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 99.65  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHaPENVELaLREFwalsSI--KSQHPNVIHLEECIlQKDGMvqkms 85
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVE-EDLQEI-IKEI----SIlkQCDSPYIVKYYGSY-FKNTD----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRkpnRKTNT----SFMLQLS-SALAFLHKNQI 160
Cdd:cd06612   73 -----------------------------LWIVMEYCGAGSVSDIMKIT---NKTLTeeeiAAILYQTlKGLEYLHSNKK 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLskvcsaSGQNPEEPVSVNkcflsTACGTDFYMAPEV-WEGHYTAKAD 239
Cdd:cd06612  121 IHRDIKAGNILLNE--------EGQAKLADFGV------SGQLTDTMAKRN-----TVIGTPFWMAPEViQEIGYNNKAD 181
                        250
                 ....*....|...
gi 119628251 240 IFALGIIIWAMLE 252
Cdd:cd06612  182 IWSLGITAIEMAE 194
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
8-322 2.78e-24

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 99.43  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGmvqkmshg 87
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDG-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRK----PNRKTNTSFMlQLSSALAFLHKNQIIHR 163
Cdd:cd08223   74 --------------------------FLYIVMGFCEGGDLYTRLKEQKgvllEERQVVEWFV-QIAMALQYMHERNILHR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd08223  127 DLKTQNIFLTKSNI--------IKVGDLGIARVLESSSD-----------MATTLIGTPYYMSPELFSNKpYNHKSDVWA 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLeriTFIDTETKKElLGSYVKQgteivpvgeaLLENPkmellIPVKKKSMNGRMKQLIKEMLAANPQDRPDA 322
Cdd:cd08223  188 LGCCVYEMA---TLKHAFNAKD-MNSLVYK----------ILEGK-----LPPMPKQYSPELGELIKAMLHQDPEKRPSV 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
8-319 2.85e-24

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 99.65  E-value: 2.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVELALREFWALSsiKSQHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILnrqKIKSLDMEEKIRREIQILK--LFRHPHIIRLYEVI---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvETslKGEIafdprsayylWFVMDFCDGGDMNEYLLSR-KPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14079   72 -------------ET--PTDI----------FMVMEYVSGGELFDYIVQKgRLSEDEARRFFQQIISGVEYCHRHMVVHR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSaSGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTA--KADIF 241
Cdd:cd14079  127 DLKPENLLL--------DSNMNVKIADFGLSNIMR-DGE-----------FLKTSCGSPNYAAPEVISGKLYAgpEVDVW 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAML-ERITFIDTET----KKELLGSYVkqgteivpvgeallenpkmellIPvkkKSMNGRMKQLIKEMLAANP 316
Cdd:cd14079  187 SCGVILYALLcGSLPFDDEHIpnlfKKIKSGIYT----------------------IP---SHLSPGARDLIKRMLVVDP 241

                 ...
gi 119628251 317 QDR 319
Cdd:cd14079  242 LKR 244
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
16-251 2.98e-24

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 99.98  E-value: 2.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  16 RGSYGVVYEAVIRKTSARVAVKKIRCH--APEN-VELALREFWALSSIksQHPNVIHLEECILQKDgmvqkmshgsnssl 92
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRdmIRKNqVDSVLAERNILSQA--QNPFVVKLYYSFQGKK-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylqlvetslkgeiafdprsayYLWFVMDFCDGGDMneYLLSRKPNR--KTNTSFML-QLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd05579   67 ---------------------NLYLVMEYLPGGDL--YSLLENVGAldEDVARIYIaEIVLALEYLHSHGIIHRDLKPDN 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISQtrldtsdlEPTLKVADFGLSKV------CSASGQNPEEPVSVNKCflSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05579  124 ILIDA--------NGHLKLTDFGLSKVglvrrqIKLSIQKKSNGAPEKED--RRIVGTPDYLAPEILLGQgHGKTVDWWS 193

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd05579  194 LGVILYEFL 202
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
14-321 4.20e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 99.31  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIR-KTSARVAVKKIRCHAPENVELAL-REFWALSSIksQHPNVIHLEEcilqkdgmVQKMshgsnss 91
Cdd:cd14201   14 VGHGAFAVVFKGRHRkKTDWEVAIKSINKKNLSKSQILLgKEIKILKEL--QHENIVALYD--------VQEM------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafdPRSAYylwFVMDFCDGGDMNEYLLSRKPNRK-TNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd14201   77 -----------------PNSVF---LVMEYCNGGDLADYLQAKGTLSEdTIRVFLQQIAAAMRILHSKGIIHRDLKPQNI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LISQTRLDTSDLEPT-LKVADFGLSKVCSASgqnpeepvsvnkCFLSTACGTDFYMAPEV-WEGHYTAKADIFALGIIIW 248
Cdd:cd14201  137 LLSYASRKKSSVSGIrIKIADFGFARYLQSN------------MMAATLCGSPMYMAPEViMSQHYDAKADLWSIGTVIY 204
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 249 AMLERITFIDTETKKELLGSYVKQGTeivpvgeallenpkmelLIPVKKKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd14201  205 QCLVGKPPFQANSPQDLRMFYEKNKN-----------------LQPSIPRETSPYLADLLLGLLQRNQKDRMD 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
7-251 6.55e-24

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 98.57  E-value: 6.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENveLALREFWALSSIKsqHPNVIHLeecilqkdgmVQK 83
Cdd:cd14184    2 KYKIGKVIGDGNFAVVKECVERSTGKEFALKiidKAKCCGKEH--LIENEVSILRRVK--HPNIIML----------IEE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MShgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSR-KPNRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd14184   68 MD--TPAELYL-----------------------VMELVKGGDLFDAITSStKYTERDASAMVYNLASALKYLHGLCIVH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldTSDLEPTLKVADFGLSKVCsasgqnpEEPvsvnkcfLSTACGTDFYMAPE-VWEGHYTAKADIF 241
Cdd:cd14184  123 RDIKPENLLVCE----YPDGTKSLKLGDFGLATVV-------EGP-------LYTVCGTPTYVAPEiIAETGYGLKVDIW 184
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14184  185 AAGVITYILL 194
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
7-253 7.17e-24

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 98.29  E-value: 7.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL---ALREFWALSSIKsqHPNVIHLEECILQKDgmvqk 83
Cdd:cd06607    2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwqdIIKEVKFLRQLR--HPNTIEYKGCYLREH----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDG--GDMNEylLSRKPNRKTNTSFM-LQLSSALAFLHKNQI 160
Cdd:cd06607   75 ------------------------------TAWLVMEYCLGsaSDIVE--VHKKPLQEVEIAAIcHGALQGLAYLHSHNR 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGlskvcSASGQNPEepvsvnkcflSTACGTDFYMAPEVW----EGHYTA 236
Cdd:cd06607  123 IHRDVKAGNILLTE--------PGTVKLADFG-----SASLVCPA----------NSFVGTPYWMAPEVIlamdEGQYDG 179
                        250
                 ....*....|....*..
gi 119628251 237 KADIFALGIIIWAMLER 253
Cdd:cd06607  180 KVDVWSLGITCIELAER 196
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
8-325 1.20e-23

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 97.76  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELA--LREFWALSSIkSQHPNVIHLEECILQKDgmvqkms 85
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKrkLEEVERHEKL-GEHPNCVRFIKAWEEKG------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsSLYLQlvetslkgeiafdprsayylwfvMDFCDGgDMNEYLL--SRKPNRKTnTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14050   75 -----ILYIQ-----------------------TELCDT-SLQQYCEetHSLPESEV-WNILLDLLKGLKHLHDHGLIHL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRldtsdlepTLKVADFGL------SKVCSASGQNPEepvsvnkcflstacgtdfYMAPEVWEGHYTAK 237
Cdd:cd14050  125 DIKPANIFLSKDG--------VCKLGDFGLvveldkEDIHDAQEGDPR------------------YMAPELLQGSFTKA 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIiiwAMLERITFIDtetkkellgsyvkqgteiVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd14050  179 ADIFSLGI---TILELACNLE------------------LPSGGDGWHQLRQGYLPEEFTAGLSPELRSIIKLMMDPDPE 237

                 ....*...
gi 119628251 318 DRPDAFEL 325
Cdd:cd14050  238 RRPTAEDL 245
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7-253 1.50e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 97.50  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELALREFWALSSIksQHPNVIHLEECILQKDGMVqkm 84
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEqmTKEERQAALNEVKVLSML--HHPNIIEYYESFLEDKALM--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKP---NRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd08220   76 --------------------------------IVMEYAPGGTLFEYIQQRKGsllSEEEILHFFVQILLALHHVHSKQIL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRLdtsdlepTLKVADFGLSKVCSAsgqnpeepvsvnKCFLSTACGTDFYMAPEVWEGH-YTAKADI 240
Cdd:cd08220  124 HRDLKTQNILLNKKRT-------VVKIGDFGISKILSS------------KSKAYTVVGTPCYISPELCEGKpYNQKSDI 184
                        250
                 ....*....|....*
gi 119628251 241 FALGIIIW--AMLER 253
Cdd:cd08220  185 WALGCVLYelASLKR 199
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
8-325 2.05e-23

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 97.37  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHAPENV--ELALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVsKKKAPEDYlqKFLPREIEVIKGLK--HPNLICFYEAI---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvETSlkgeiafdprSAYYLwfVMDFCDGGDMNEYLLSRK--PNRKTNTSFMlQLSSALAFLHKNQIIH 162
Cdd:cd14162   70 -------------ETT----------SRVYI--IMELAENGDLLDYIRKNGalPEPQARRWFR-QLVAGVEYCHSKGVVH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILisqtrLDTSDlepTLKVADFGLSKVCSasgqnpeEPVSVNKCFLSTACGTDFYMAPEVWEG-HYTAK-ADI 240
Cdd:cd14162  124 RDLKCENLL-----LDKNN---NLKITDFGFARGVM-------KTKDGKPKLSETYCGSYAYASPEILRGiPYDPFlSDI 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAML-ERITFIDTETKKellgsyvkqgteivpvgeaLLENPKMELLIPvKKKSMNGRMKQLIKEMLAANPQdR 319
Cdd:cd14162  189 WSMGVVLYTMVyGRLPFDDSNLKV-------------------LLKQVQRRVVFP-KNPTVSEECKDLILRMLSPVKK-R 247

                 ....*.
gi 119628251 320 PDAFEL 325
Cdd:cd14162  248 ITIEEI 253
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
6-324 6.93e-23

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 97.54  E-value: 6.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSsiKSQHPNVIHLEECI------LQKDg 79
Cdd:cd07854    5 SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIR--RLDHDNIVKVYEVLgpsgsdLTED- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 mVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLwfvmdfcdggdmneyllsrkpnrktnTSFMLQLSSALAFLHKNQ 159
Cdd:cd07854   82 -VGSLTELNSVYIVQEYMETDLANVLEQGPLSEEHA--------------------------RLFMYQLLRGLKYIHSAN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRLdtsdlepTLKVADFGLSKVCsasgqnpeEPVSVNKCFLSTACGTDFYMAPEVW--EGHYTAK 237
Cdd:cd07854  135 VLHRDLKPANVFINTEDL-------VLKIGDFGLARIV--------DPHYSHKGYLSEGLVTKWYRSPRLLlsPNNYTKA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAM-------------------LERITFIDTETKKELLG---SYVKQGTEIVpvgeallENPKMELLIPV 295
Cdd:cd07854  200 IDMWAAGCIFAEMltgkplfagaheleqmqliLESVPVVREEDRNELLNvipSFVRNDGGEP-------RRPLRDLLPGV 272
                        330       340
                 ....*....|....*....|....*....
gi 119628251 296 KKKSMNgrmkqLIKEMLAANPQDRPDAFE 324
Cdd:cd07854  273 NPEALD-----FLEQILTFNPMDRLTAEE 296
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
8-251 8.21e-23

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 95.56  E-value: 8.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELA--LREFWALSSIksQHPNVIHLEECIlqkdgmvqkms 85
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAhlFQEVRCMKLV--QHPNVVRLYEVI----------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvETSLKgeiafdprsayyLWFVMDFCDGGDMNEYLLS--RKPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14074   72 ------------DTQTK------------LYLILELGDGGDMYDYIMKheNGLNEDLARKYFRQIVSAISYCHKLHVVHR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdlEPTLKVADFGLSKvCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG-HYTAKA-DIF 241
Cdd:cd14074  128 DLKPENVVFFEK-------QGLVKLTDFGFSN-KFQPGEK-----------LETSCGSLAYSAPEILLGdEYDAPAvDIW 188
                        250
                 ....*....|
gi 119628251 242 ALGIIIWaML 251
Cdd:cd14074  189 SLGVILY-ML 197
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
8-251 8.58e-23

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 97.36  E-value: 8.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKirchapenvelaLREFWALSSIKSQHpnvIHLEecilqKDGMVQkmshg 87
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKI------------LRKSDMLKREQIAH---VRAE-----RDILAD----- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQLVetslkgeIAF-DPRsayYLWFVMDFCDGGDMnEYLLSRKpNRKTNTS---FMLQLSSALAFLHKNQIIHR 163
Cdd:cd05573   58 ADSPWIVRLH-------YAFqDED---HLYLVMEYMPGGDL-MNLLIKY-DVFPEETarfYIAELVLALDSLHKLGFIHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSK------------------VCSASGQNPEEPVSVNKCFLSTACGTDFYM 225
Cdd:cd05573  126 DIKPDNILL--------DADGHIKLADFGLCTkmnksgdresylndsvntLFQDNVLARRRPHKQRRVRAYSAVGTPDYI 197
                        250       260
                 ....*....|....*....|....*..
gi 119628251 226 APEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05573  198 APEVLRGTgYGPECDWWSLGVILYEML 224
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
8-251 1.07e-22

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 95.72  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH---APENVELALREFWALSSIksQHPNVIHLeecilqkdgmvqkm 84
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAkiiKLKQVEHVLNEKRILSEV--RHPFIVNL-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 sHGSnsslylqlvetslkgeiaF-DPRsayYLWFVMDFCDGGDMNEYLlsRKPNRKTNTSFML---QLSSALAFLHKNQI 160
Cdd:cd05580   67 -LGS------------------FqDDR---NLYMVMEYVPGGELFSLL--RRSGRFPNDVAKFyaaEVVLALEYLHSLDI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCsasgqnpeepvsVNKCFlsTACGTDFYMAPEVWEGH-YTAKAD 239
Cdd:cd05580  123 VYRDLKPENLLL--------DSDGHIKITDFGFAKRV------------KDRTY--TLCGTPEYLAPEIILSKgHGKAVD 180
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd05580  181 WWALGILIYEML 192
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
8-250 1.29e-22

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 95.44  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHAPEnvelALREFWALSSIKsqHPNVIHLEECilqkdgmvqkmsh 86
Cdd:cd14010    2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVdKSKRPE----VLNEVRLTHELK--HPNVLKFYEW------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslYlqlvETSlkgeiafdprsaYYLWFVMDFCDGGDMnEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14010   63 ------Y----ETS------------NHLWLVVEYCTGGDL-ETLLRQDGNLPESSvrKFGRDLVRGLHYIHSKGIIYCD 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILisqtrLDtsdlEP-TLKVADFGLSKVC-----SASGQNPEEPVSVNKCFLSTACGTDFYMAPEVW-EGHYTAK 237
Cdd:cd14010  120 LKPSNIL-----LD----GNgTLKLSDFGLARREgeilkELFGQFSDEGNVNKVSKKQAKRGTPYYMAPELFqGGVHSFA 190
                        250
                 ....*....|...
gi 119628251 238 ADIFALGIIIWAM 250
Cdd:cd14010  191 SDLWALGCVLYEM 203
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
14-332 2.65e-22

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 94.65  E-value: 2.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSArVAVKKIR---CHAPEnvELALREFWALSsiKSQHPNVIHLEECILQKDGMVqkmshgsns 90
Cdd:cd14066    1 IGSGGFGTVYKGVLENGTV-VAVKRLNemnCAASK--KEFLTELEMLG--RLRHPNLVRLLGYCLESDEKL--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKPNR----KTNTSFMLQLSSALAFLH---KNQIIHR 163
Cdd:cd14066   67 --------------------------LVYEYMPNGSLEDRLHCHKGSPplpwPQRLKIAKGIARGLEYLHeecPPPIIHG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILisqtrLDtSDLEPtlKVADFGLSKVcsasgQNPEEPVSVNkcflSTACGTDFYMAPE-VWEGHYTAKADIFA 242
Cdd:cd14066  121 DIKSSNIL-----LD-EDFEP--KLTDFGLARL-----IPPSESVSKT----SAVKGTIGYLAPEyIRTGRVSTKSDVYS 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIiwaMLERIT---FIDTETKKELLGSyvkqGTEIVpvgEALLENPKMELL---IPVKKKSMNGRMKQLIK---EMLA 313
Cdd:cd14066  184 FGVV---LLELLTgkpAVDENRENASRKD----LVEWV---ESKGKEELEDILdkrLVDDDGVEEEEVEALLRlalLCTR 253
                        330
                 ....*....|....*....
gi 119628251 314 ANPQDRPDAFELELRLVQI 332
Cdd:cd14066  254 SDPSLRPSMKEVVQMLEKL 272
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
8-251 3.73e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 94.74  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRChapENVE-----LALREFWALSSIKsqHPNVIHLEECILQKdgmvq 82
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRM---DNERdgipiSSLREITLLLNLR--HPNIVELKEVVVGK----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEyLLSRKPNRKTNT---SFMLQLSSALAFLHKNQ 159
Cdd:cd07845   79 -----HLDSIFL-----------------------VMEYCEQ-DLAS-LLDNMPTPFSESqvkCLMLQLLRGLQYLHENF 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSaSGQNPEEPVSVnkcflstacgTDFYMAPEVWEG--HYTAK 237
Cdd:cd07845  129 IIHRDLKVSNLLLTDKGC--------LKIADFGLARTYG-LPAKPMTPKVV----------TLWYRAPELLLGctTYTTA 189
                        250
                 ....*....|....
gi 119628251 238 ADIFALGIIIWAML 251
Cdd:cd07845  190 IDMWAVGCILAELL 203
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
15-325 3.80e-22

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 94.36  E-value: 3.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELA--LREFWALSSIksQHPNVIHLEECILQKDGMVQKMSHGSNSSL 92
Cdd:cd14046   15 GKGAFGQVVKVRNKLDGRYYAIKKIK-LRSESKNNSriLREVMLLSRL--NHQHVVRYYQAWIERANLYIQMEYCEKSTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 YlQLVETSLkgeiaFDPRSAYYLWFvmdfcdggdmneyllsrkpnRktntsfmlQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14046   92 R-DLIDSGL-----FQDTDRLWRLF--------------------R--------QILEGLAYIHSQGIIHRDLKPVNIFL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 sqtrlDTSDlepTLKVADFGLSK----VCSASGQNPEEPVSVNKCF---LSTACGTDFYMAPEV---WEGHYTAKADIFA 242
Cdd:cd14046  138 -----DSNG---NVKIGDFGLATsnklNVELATQDINKSTSAALGSsgdLTGNVGTALYVAPEVqsgTKSTYNEKVDMYS 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAM-------LERITFIDTetkkellgsyvkqgteivpvgealLENPKMElLIPVKKKSMNGRMKQLIKEMLAAN 315
Cdd:cd14046  210 LGIIFFEMcypfstgMERVQILTA------------------------LRSVSIE-FPPDFDDNKHSKQAKLIRWLLNHD 264
                        330
                 ....*....|
gi 119628251 316 PQDRPDAFEL 325
Cdd:cd14046  265 PAKRPSAQEL 274
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
8-319 4.01e-22

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 93.69  E-value: 4.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHAPEN-VELAL-REFWALSSIKsqHPNVIHLEECILQKDGmvqkm 84
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIdKKKAPDDfVEKFLpRELEILARLN--HKSIIKTYEIFETSDG----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSR-KPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14165   76 -----------------------------KVYIVMELGVQGDLLEFIKLRgALPEDVARKMFHQLSSAIKYCHELDIVHR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGqNPEEPVSvnkcflSTACGTDFYMAPEVWEGH-YTAKA-DIF 241
Cdd:cd14165  127 DLKCENLLL--------DKDFNIKLTDFGFSKRCLRDE-NGRIVLS------KTFCGSAAYAAPEVLQGIpYDPRIyDIW 191
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 242 ALGIIIWAML-ERITFIDTETKKellgsyvkqgteivpvgeALLENPKMELLIPvKKKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14165  192 SLGVILYIMVcGSMPYDDSNVKK------------------MLKIQKEHRVRFP-RSKNLTSECKDLIYRLLQPDVSQR 251
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7-322 4.30e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 93.50  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVELALREFWALSSIKsqHPNVIHLEECiLQKDGmvqkms 85
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLpKSSSAVEDSRKEAVLLAKMK--HPNIVAFKES-FEADG------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPN---RKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd08219   72 ----------------------------HLYIVMEYCDGGDLMQKIKLQRGKlfpEDTILQWFVQMCLGVQHIHEKRVLH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSasgqnpeEPVSvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd08219  124 RDIKSKNIFLTQN--------GKVKLGDFGSARLLT-------SPGA----YACTYVGTPYYVPPEIWENMpYNNKSDIW 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWamleritfidtetkkellgsyvkqgtEIVPVGEALLENPKMELLIPVKKKSMNG-------RMKQLIKEMLAA 314
Cdd:cd08219  185 SLGCILY--------------------------ELCTLKHPFQANSWKNLILKVCQGSYKPlpshysyELRSLIKQMFKR 238

                 ....*...
gi 119628251 315 NPQDRPDA 322
Cdd:cd08219  239 NPRSRPSA 246
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7-251 4.33e-22

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 93.59  E-value: 4.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALR-EFWALSSIKsqHPNVIHLEEcilqkdgmvqkms 85
Cdd:cd14083    4 KYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLEnEIAVLRKIK--HPNIVQLLD------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14083   69 --------------------IYESKSHLYL--VMELVTGGELFDRIVEKGSyTEKDASHLIRQVLEAVDYLHSLGIVHRD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldTSDLEPTLKVADFGLSKVcSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTAKA-DIFAL 243
Cdd:cd14083  127 LKPENLLYY-----SPDEDSKIMISDFGLSKM-EDSG------------VMSTACGTPGYVAPEVLAQKPYGKAvDCWSI 188

                 ....*...
gi 119628251 244 GIIIWAML 251
Cdd:cd14083  189 GVISYILL 196
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
7-252 1.11e-21

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 92.68  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHleecilqkdgmvqkmsh 86
Cdd:cd06647    8 KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENK--NPNIVN----------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslYLqlvETSLKGEiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd06647   69 ------YL---DSYLVGD---------ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISqtrldtsdLEPTLKVADFGLSKVCSasgqnPEEpvsvNKcfLSTACGTDFYMAPE-VWEGHYTAKADIFALGI 245
Cdd:cd06647  131 SDNILLG--------MDGSVKLTDFGFCAQIT-----PEQ----SK--RSTMVGTPYWMAPEvVTRKAYGPKVDIWSLGI 191

                 ....*..
gi 119628251 246 IIWAMLE 252
Cdd:cd06647  192 MAIEMVE 198
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
15-321 1.19e-21

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 92.32  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVK--------KIRChAPENVElalREFWALSSIKsqHPNVIHLEECILQKDGmvQKMsh 86
Cdd:cd14119    2 GEGSYGKVKEVLDTETLCRRAVKilkkrklrRIPN-GEANVK---REIQILRRLN--HRNVIKLVDVLYNEEK--QKL-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayylWFVMDFCDGGdMNEYLLSRKPNR---KTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14119   72 -----------------------------YMVMEYCVGG-LQEMLDSAPDKRlpiWQAHGYFVQLIDGLEYLHSQGIIHK 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldtsdLEPTLKVADFGLSKVCSASGQNPEepvsvnkcfLSTACGTDFYMAPEVWEGHYT---AKADI 240
Cdd:cd14119  122 DIKPGNLLLT--------TDGTLKISDFGVAEALDLFAEDDT---------CTTSQGSPAFQPPEIANGQDSfsgFKVDI 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLEritfidtetkkellGSYVKQGTEIVpvgeALLEN-PKMELLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14119  185 WSAGVTLYNMTT--------------GKYPFEGDNIY----KLFENiGKGEYTIP---DDVDPDLQDLLRGMLEKDPEKR 243

                 ..
gi 119628251 320 PD 321
Cdd:cd14119  244 FT 245
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
8-250 1.43e-21

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 92.07  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHA-PENVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkms 85
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIdKSQLdEENLKKIYREVQIMKMLN--HPHIIKL--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslyLQLVETSlkgeiafdprsaYYLWFVMDFCDGGDMNEYLLS--RKPNRKTNTSFMlQLSSALAFLHKNQIIHR 163
Cdd:cd14071   65 --------YQVMETK------------DMLYLVTEYASNGEIFDYLAQhgRMSEKEARKKFW-QILSAVEYCHKRHIVHR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKVcsasgQNPEEPvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd14071  124 DLKAENLLL--------DANMNIKIADFGFSNF-----FKPGEL-------LKTWCGSPPYAAPEVFEGkeYEGPQLDIW 183

                 ....*....
gi 119628251 242 ALGIIIWAM 250
Cdd:cd14071  184 SLGVVLYVL 192
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-319 1.62e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 92.75  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVA---VKKIRCHAPENVElalREFWALSSIKsqHPNVIHLEECilqkdgmvqkm 84
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYAlkcIKKSPLSRDSSLE---NEIAVLKRIK--HENIVTLEDI----------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd14166   69 ----------------------YESTTHYYL--VMQLVSGGELFDRILERGVYTEKDASRVInQVLSAVKYLHENGIVHR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldTSDLEPTLKVADFGLSKVcSASGqnpeepvsvnkcFLSTACGTDFYMAPEVW-EGHYTAKADIFA 242
Cdd:cd14166  125 DLKPENLLYL-----TPDENSKIMITDFGLSKM-EQNG------------IMSTACGTPGYVAPEVLaQKPYSKAVDCWS 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 243 LGIIIWAMLERITFIDTETKKELLgsyvkqgtEIVPVGEALLENPKMEllipvkkkSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14166  187 IGVITYILLCGYPPFYEETESRLF--------EKIKEGYYEFESPFWD--------DISESAKDFIRHLLEKNPSKR 247
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
8-246 1.72e-21

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 92.67  E-value: 1.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHapENVE----LALREFWALSSIksQHPNVIHLEECILqkdgmvqk 83
Cdd:cd07843    7 YEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKME--KEKEgfpiTSLREINILLKL--QHPNIVTVKEVVV-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshGSNS-SLYL--QLVETSLKGeiafdprsayylwfVMDfcdggDMNEYLLsrKPNRKTntsFMLQLSSALAFLHKNQI 160
Cdd:cd07843   75 ---GSNLdKIYMvmEYVEHDLKS--------------LME-----TMKQPFL--QSEVKC---LMLQLLSGVAHLHDNWI 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVW--EGHYTAKA 238
Cdd:cd07843  128 LHRDLKTSNLLLNNRGI--------LKICDFGLAREYGSPLKPYTQLVV-----------TLWYRAPELLlgAKEYSTAI 188

                 ....*...
gi 119628251 239 DIFALGII 246
Cdd:cd07843  189 DMWSVGCI 196
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
8-321 1.85e-21

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 91.63  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHApENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKildKTKLDQ-KTQRLLSREISSMEKL--HHPNIIRLYE------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqLVETSLKgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd14075   69 -----------VVETLSK------------LHLVMEYASGGELYTKISTEGKLSESEAKPLFaQIVSAVKHMHENNIIHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldtsdLEPTLKVADFGLSKVCsasgqNPEEPvsvnkcfLSTACGTDFYMAPEVW--EGHYTAKADIF 241
Cdd:cd14075  126 DLKAENVFYA--------SNNCVKVGDFGFSTHA-----KRGET-------LNTFCGSPPYAAPELFkdEHYIGIYVDIW 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTET----KKELL-GSYVkqgteiVP--VGEAllenpkmellipvkkksmngrMKQLIKEMLAA 314
Cdd:cd14075  186 ALGVLLYFMVTGVMPFRAETvaklKKCILeGTYT------IPsyVSEP---------------------CQELIRGILQP 238

                 ....*..
gi 119628251 315 NPQDRPD 321
Cdd:cd14075  239 VPSDRYS 245
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
8-251 2.16e-21

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 91.68  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA-PENVELALREFWALSSIKSQHpnvihleecILQkdgmvqkmsh 86
Cdd:cd14078    5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlGDDLPRVKTEIEALKNLSHQH---------ICR---------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnssLYlQLVETSLKgeiafdprsayyLWFVMDFCDGGDMNEYLLSRkpNRKTNTS---FMLQLSSALAFLHKNQIIHR 163
Cdd:cd14078   66 -----LY-HVIETDNK------------IFMVLEYCPGGELFDYIVAK--DRLSEDEarvFFRQIVSAVAYVHSQGYAHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLskvCSasgqnpeEPVSVNKCFLSTACGTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd14078  126 DLKPENLLL--------DEDQNLKLIDFGL---CA-------KPKGGMDHHLETCCGSPAYAAPELIQGkpYIGSEADVW 187
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14078  188 SMGVLLYALL 197
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
8-322 2.19e-21

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 91.46  E-value: 2.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVE-LALREFWALSSIKsqHPNVIHLEECILQKDGMVQKM 84
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVdrRRASPDFVQkFLPRELSILRRVN--HPNIVQMFECIEVANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLyLQLVETslkgeiafdprsayylwfvmdfcdggdmneylLSRKPNRKTNTSFMlQLSSALAFLHKNQIIHRD 164
Cdd:cd14164   80 MEAAATDL-LQKIQE--------------------------------VHHIPKDLARDMFA-QMVGAVNYLHDMNIVHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTrldtsdlEPTLKVADFGLSKVCSASgqnPEepvsvnkcfLSTA-CGTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd14164  126 LKCENILLSAD-------DRKIKIADFGFARFVEDY---PE---------LSTTfCGSRAYTPPEVILGtpYDPKKYDVW 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLeritfidtetkkellgsyvkqgTEIVPVGEALLENPKME---LLIPvKKKSMNGRMKQLIKEMLAANPQD 318
Cdd:cd14164  187 SLGVVLYVMV----------------------TGTMPFDETNVRRLRLQqrgVLYP-SGVALEEPCRALIRTLLQFNPST 243

                 ....
gi 119628251 319 RPDA 322
Cdd:cd14164  244 RPSI 247
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
7-319 2.34e-21

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 91.55  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAviRKTSAR-VAVKKIRCHAPENVELAL---REFWALSSIksQHPNVIHLEECILQKDGMVq 82
Cdd:cd14161    4 RYEFLETLGKGTYGRVKKA--RDSSGRlVAIKSIRKDRIKDEQDLLhirREIEIMSSL--NHPHIISVYEVFENSSKIV- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQII 161
Cdd:cd14161   79 ----------------------------------IVMEYASRGDLYDYISERQRLSELEARhFFRQIVSAVHYCHANGIV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTA-KAD 239
Cdd:cd14161  125 HRDLKLENILL--------DANGNIKIADFGLSNLYNQDK------------FLQTYCGSPLYASPEIVNGRpYIGpEVD 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERITFIDTETKKELL-----GSYVKqgteivpvgeallenpkmelliPVKKKSMNGrmkqLIKEMLAA 314
Cdd:cd14161  185 SWSLGVLLYILVHGTMPFDGHDYKILVkqissGAYRE----------------------PTKPSDACG----LIRWLLMV 238

                 ....*
gi 119628251 315 NPQDR 319
Cdd:cd14161  239 NPERR 243
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
7-251 3.05e-21

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 91.65  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--------RCHAPENVELALREFWALSSIkSQHPNVIHLEECIlqkd 78
Cdd:cd14093    4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIditgekssENEAEELREATRREIEILRQV-SGHPNIIELHDVF---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkmshgsnsslylqlvETSLkgeiafdprsayYLWFVMDFCDGGDMNEYL-----LSRKPNRKTntsfMLQLSSALA 153
Cdd:cd14093   79 -------------------ESPT------------FIFLVFELCRKGELFDYLtevvtLSEKKTRRI----MRQLFEAVE 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 154 FLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCsasgqNPEEpvsvnkcFLSTACGTDFYMAPEV---- 229
Cdd:cd14093  124 FLHSLNIVHRDLKPENILL--------DDNLNVKISDFGFATRL-----DEGE-------KLRELCGTPGYLAPEVlkcs 183
                        250       260
                 ....*....|....*....|....*
gi 119628251 230 -WEGH--YTAKADIFALGIIIWAML 251
Cdd:cd14093  184 mYDNApgYGKEVDMWACGVIMYTLL 208
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
7-256 3.74e-21

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 91.13  E-value: 3.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDliREVGRGSYGVVYEAVIRKTSARVA--VKKIRCHAPENVELALREFWALSSIksQHPNVIHLeecilqkdgmvqkm 84
Cdd:cd13983    4 KFN--EVLGRGSFKTVYRAFDTEEGIEVAwnEIKLRKLPKAERQRFKQEIEILKSL--KHPNIIKF-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 sHGSnsslylqlVETSLKGEIAFdprsayylwfVMDFCDGGDMNEYLL-SRKPNRKTNTSFMLQLSSALAFLHKNQ--II 161
Cdd:cd13983   66 -YDS--------WESKSKKEVIF----------ITELMTSGTLKQYLKrFKRLKLKVIKSWCRQILEGLNYLHTRDppII 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTRLDtsdleptLKVADFGLSKVCSASgqnpeEPVSVNkcflstacGTDFYMAPEVWEGHYTAKADIF 241
Cdd:cd13983  127 HRDLKCDNIFINGNTGE-------VKIGDLGLATLLRQS-----FAKSVI--------GTPEFMAPEMYEEHYDEKVDIY 186
                        250
                 ....*....|....*
gi 119628251 242 ALGIiiwAMLERITF 256
Cdd:cd13983  187 AFGM---CLLEMATG 198
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
7-324 5.00e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 91.18  E-value: 5.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN-VELA-LREFWALSSIKS-QHPNVIHLEE-CILQKDGMVQ 82
Cdd:cd07863    1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDgLPLStVREVALLKRLEAfDHPNIVRLMDvCATSRTDRET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMShgsnssLYLQLVETSLKGEIAFDPRSAYYLWFVMDFcdggdmneyllsrkpnrktntsfMLQLSSALAFLHKNQIIH 162
Cdd:cd07863   81 KVT------LVFEHVDQDLRTYLDKVPPPGLPAETIKDL-----------------------MRQFLRGLDFLHANCIVH 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSAsgQNPEEPVSVnkcflstacgTDFYMAPEV-WEGHYTAKADIF 241
Cdd:cd07863  132 RDLKPENILVTS--------GGQVKLADFGLARIYSC--QMALTPVVV----------TLWYRAPEVlLQSTYATPVDMW 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELLGSYVK----QGTEIVPVGEALLEN---PKMELliPVKK--KSMNGRMKQLIKEML 312
Cdd:cd07863  192 SVGCIFAEMFRRKPLFCGNSEADQLGKIFDliglPPEDDWPRDVTLPRGafsPRGPR--PVQSvvPEIEESGAQLLLEML 269
                        330
                 ....*....|..
gi 119628251 313 AANPQDRPDAFE 324
Cdd:cd07863  270 TFNPHKRISAFR 281
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
11-253 5.16e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 91.03  E-value: 5.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA-PENV-ELALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkmsHgS 88
Cdd:cd07860    5 VEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTeTEGVpSTAIREISLLKELN--HPNIVKLLDVI-----------H-T 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYL--QLVETSLKGeiafdprsayylwfVMDFCDGGDMNEYLLSrkpnrktntSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd07860   71 ENKLYLvfEFLHQDLKK--------------FMDASALTGIPLPLIK---------SYLFQLLQGLAFCHSHRVLHRDLK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKADIFALG 244
Cdd:cd07860  128 PQNLLI--------NTEGAIKLADFGLARAFGVPVRTYTHEVV-----------TLWYRAPEILLGckYYSTAVDIWSLG 188

                 ....*....
gi 119628251 245 IIIWAMLER 253
Cdd:cd07860  189 CIFAEMVTR 197
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-251 5.63e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 90.86  E-value: 5.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALR-EFWALSSIKsqHPNVIHLEECilqkdgmvqkmsH 86
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIEnEIAVLHKIK--HPNIVALDDI------------Y 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRK-PNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd14167   71 ESGGHLYL-----------------------IMQLVSGGELFDRIVEKGfYTERDASKLIFQILDAVKYLHDMGIVHRDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISqtrldTSDLEPTLKVADFGLSKVcsasgqnpEEPVSVnkcfLSTACGTDFYMAPEVW-EGHYTAKADIFALG 244
Cdd:cd14167  128 KPENLLYY-----SLDEDSKIMISDFGLSKI--------EGSGSV----MSTACGTPGYVAPEVLaQKPYSKAVDCWSIG 190

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd14167  191 VIAYILL 197
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
7-251 6.32e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 90.89  E-value: 6.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENV--ELALREFWALSSIKsqHPNVIHLEECILQKdgmvqkm 84
Cdd:cd07847    2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVikKIALREIRMLKQLK--HPNLVNLIEVFRRK------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEylLSRKPN---RKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd07847   73 -----RKLHL-----------------------VFEYCDHTVLNE--LEKNPRgvpEHLIKKIIWQTLQAVNFCHKHNCI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKAD 239
Cdd:cd07847  123 HRDVKPENILITK--------QGQIKLCDFGFARILTGPGDDYTDYVA-----------TRWYRAPELLVGdtQYGPPVD 183
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd07847  184 VWAIGCVFAELL 195
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
15-251 6.46e-21

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 91.68  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSsIKSQHPNVIHLEeCILQKDGmvqkmshgsnss 91
Cdd:cd05592    4 GKGSFGKVMLAELKGTNQYFAIKALKKDVvleDDDVECTMIERRVLA-LASQHPFLTHLF-CTFQTES------------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafdprsayYLWFVMDFCDGGD-MNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd05592   70 ----------------------HLFFVMEYLNGGDlMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNV 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpEEPVSVNKCflSTACGTDFYMAPEVWEG-HYTAKADIFALGIIIWA 249
Cdd:cd05592  128 LL--------DREGHIKIADFGMCK---------ENIYGENKA--STFCGTPDYIAPEILKGqKYNQSVDWWSFGVLLYE 188

                 ..
gi 119628251 250 ML 251
Cdd:cd05592  189 ML 190
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
8-325 6.57e-21

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 91.25  E-value: 6.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSikSQHPNVIhleecilqkdgmvqkmshg 87
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILAT--CNHPYIV------------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetSLKGEIAFDPRsayyLWFVMDFCDGGDMNEYLLS-----RKPNRKTNTSFMLQlssALAFLHKNQIIH 162
Cdd:cd06644   73 ------------KLLGAFYWDGK----LWIMIEFCPGGAVDAIMLEldrglTEPQIQVICRQMLE---ALQYLHSMKIIH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISqtrldtsdLEPTLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPEVW------EGHYTA 236
Cdd:cd06644  134 RDLKAGNVLLT--------LDGDIKLADFGVSAKNVKTLQRRDSFI-----------GTPYWMAPEVVmcetmkDTPYDY 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMleritfidtetkkellgsyvkqgTEIVPVGEALleNPkMELLIPVKKKSMNG---------RMKQL 307
Cdd:cd06644  195 KADIWSLGITLIEM-----------------------AQIEPPHHEL--NP-MRVLLKIAKSEPPTlsqpskwsmEFRDF 248
                        330
                 ....*....|....*...
gi 119628251 308 IKEMLAANPQDRPDAFEL 325
Cdd:cd06644  249 LKTALDKHPETRPSAAQL 266
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
110-251 6.77e-21

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 90.36  E-value: 6.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 110 RSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKV 188
Cdd:cd05572   63 KDKKYLYMLMEYCLGGELWTILRDRGLFDEYTARFYTaCVVLAFEYLHSRGIIYRDLKPENLLL--------DSNGYVKL 134
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 189 ADFGLSKVCSasgqnpeepvSVNKCFlsTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05572  135 VDFGFAKKLG----------SGRKTW--TFCGTPEYVAPEIILNKgYDFSVDYWSLGILLYELL 186
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
8-265 7.30e-21

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 90.05  E-value: 7.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHAPEN-VELAL-REFWALSSIksQHPNVIHLEECILQKDGMVqkm 84
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIdKSGGPEEfIQRFLpRELQIVERL--DHKNIIHVYEMLESADGKI--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayylWFVMDFCDGGDMNEYLLSRKPNRKTNT-SFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14163   77 -------------------------------YLVMELAEDGDVFDCVLHGGPLPEHRAkALFRQLVEAIRYCHGCGVAHR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsQTRldtsdlepTLKVADFGLSKVCSASGQNPEEpvsvnkcflsTACGTDFYMAPEVWEG--HYTAKADIF 241
Cdd:cd14163  126 DLKCENALL-QGF--------TLKLTDFGFAKQLPKGGRELSQ----------TFCGSTAYAAPEVLQGvpHDSRKGDIW 186
                        250       260
                 ....*....|....*....|....*
gi 119628251 242 ALGIIIWAML-ERITFIDTETKKEL 265
Cdd:cd14163  187 SMGVVLYVMLcAQLPFDDTDIPKML 211
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7-251 8.04e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 90.26  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELALREFWALSSIKsqHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd08218    1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISkmSPKEREESRKEVAVLSKMK--HPNIVQYQE------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRK----PNRKTnTSFMLQLSSALAFLHKNQI 160
Cdd:cd08218   67 SFEENGNLYI-----------------------VMDYCDGGDLYKRINAQRgvlfPEDQI-LDWFVQLCLALKHVHDRKI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTAC-GTDFYMAPEVWEGH-YTAKA 238
Cdd:cd08218  123 LHRDIKSQNIFLTK--------DGIIKLGDFGIARVLNSTVE------------LARTCiGTPYYLSPEICENKpYNNKS 182
                        250
                 ....*....|...
gi 119628251 239 DIFALGIIIWAML 251
Cdd:cd08218  183 DIWALGCVLYEMC 195
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
14-332 8.23e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 90.05  E-value: 8.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIRcHAP--------ENVELALREFWALssiksQHPNVIhleecilqkdgmvqkms 85
Cdd:cd14148    2 IGVGGFGKVYKGLWR--GEEVAVKAAR-QDPdediavtaENVRQEARLFWML-----QHPNII----------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetSLKGEIAFDPrsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQ---IIH 162
Cdd:cd14148   57 --------------ALRGVCLNPP----HLCLVMEYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIH 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtRLDTSDL-EPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTACGTDFYMAPEVWE-GHYTAKADI 240
Cdd:cd14148  119 RDLKSSNILILE-PIENDDLsGKTLKITDFGLAR-------------EWHKTTKMSAAGTYAWMAPEVIRlSLFSKSSDV 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLEritfidtetkkellGSYVKQGTEIVPVGEALLENpKMELLIPvkkKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14148  185 WSFGVLLWELLT--------------GEVPYREIDALAVAYGVAMN-KLTLPIP---STCPEPFARLLEECWDPDPHGRP 246
                        330
                 ....*....|..
gi 119628251 321 DAFELELRLVQI 332
Cdd:cd14148  247 DFGSILKRLEDI 258
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
8-270 8.31e-21

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 90.96  E-value: 8.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSAR-VAVKKIRCHAPENVELAlrefwalssiKSQHPNVihLEEcilqkdgmVQKMSH 86
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPLRNTGKpVAIKVVRKADLSSDNLK----------GSSRANI--LKE--------VQIMKR 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLyLQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDM-NEYL--------LSRKpnrktntsFMLQLSSALAFLHK 157
Cdd:cd14096   63 LSHPNI-VKLLDF-------QESDEYYYI--VLELADGGEIfHQIVrltyfsedLSRH--------VITQVASAVKYLHE 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIS-----------------QTRLDTSDLEP--------TLKVADFGLSKVCSASGqnpeepvsvnk 212
Cdd:cd14096  125 IGVVHRDIKPENLLFEpipfipsivklrkadddETKVDEGEFIPgvggggigIVKLADFGLSKQVWDSN----------- 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 213 cfLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAMLerITF-------IDTETKKELLGSYV 270
Cdd:cd14096  194 --TKTPCGTVGYTAPEVVkDERYSKKVDMWALGCVLYTLL--CGFppfydesIETLTEKISRGDYT 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
12-251 9.66e-21

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 89.72  E-value: 9.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRChAPENVElALREFWALSsiksqhpNVIHLEECiLQKDGMVQkmshgsnss 91
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEI-DPINTE-ASKEVKALE-------CEIQLLKN-LQHERIVQ--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lYLQLVEtslkgeiafDPRSayyLWFVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd06625   67 -YYGCLQ---------DEKS---LSIFMEYMPGGSVKDEIkaygaLTENVTRK----YTRQILEGLAYLHSNMIVHRDIK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILisqtrldtSDLEPTLKVADFGLSK----VCSASGqnpeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd06625  130 GANIL--------RDSNGNVKLGDFGASKrlqtICSSTG-------------MKSVTGTPYWMSPEVINGEgYGRKADIW 188
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd06625  189 SVGCTVVEML 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
12-322 1.10e-20

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 90.02  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYG-VVYEAVIRKTsaRVAVKKIrchAPENVELALREFWALssIKS-QHPNVIHLEeCiLQKDGMVQKMShgsn 89
Cdd:cd13982    7 KVLGYGSEGtIVFRGTFDGR--PVAVKRL---LPEFFDFADREVQLL--RESdEHPNVIRYF-C-TEKDRQFLYIA---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sslyLQLVETSLKgeiafdprsayylwfvmDFCDGGDMNEYLLSRKPNRKTntsFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd13982   74 ----LELCAASLQ-----------------DLVESPRESKLFLRPGLEPVR---LLRQIASGLAHLHSLNIVHRDLKPQN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISqtrLDTSDLEPTLKVADFGLSKVCSAsGQNpeepvSVNKcfLSTACGTDFYMAPEVWEGHY----TAKADIFALGI 245
Cdd:cd13982  130 ILIS---TPNAHGNVRAMISDFGLCKKLDV-GRS-----SFSR--RSGVAGTSGWIAPEMLSGSTkrrqTRAVDIFSLGC 198
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 246 IIWAMLeritfidTETKKELLGSYVKQGTeivpvgeaLLENpKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRPDA 322
Cdd:cd13982  199 VFYYVL-------SGGSHPFGDKLEREAN--------ILKG-KYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSA 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
7-265 1.12e-20

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 89.90  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVELALRefwALSSIKsqHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14087    2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIetKCRGREVCESELN---VLRRVR--HTNIIQLIE------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHR 163
Cdd:cd14087   65 ---------------------VFETKERVYM--VMELATGGELFDRIIAKGSFTERDATRVLQmVLDGVKYLHGLGITHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRLDTSdleptLKVADFGLSkvcSASGQNPEepvsvnkCFLSTACGTDFYMAPEVW-EGHYTAKADIFA 242
Cdd:cd14087  122 DLKPENLLYYHPGPDSK-----IMITDFGLA---STRKKGPN-------CLMKTTCGTPEYIAPEILlRKPYTQSVDMWA 186
                        250       260
                 ....*....|....*....|...
gi 119628251 243 LGIIIWAMLERITFIDTETKKEL 265
Cdd:cd14087  187 VGVIAYILLSGTMPFDDDNRTRL 209
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
7-253 1.17e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 90.17  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN--VELALREFWALSSIksQHPNVIHLEECILQKdgmvqkm 84
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKEL--QHPNIVCLEDVLMQE------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnSSLYLqlvetslkgeiafdprsayylwfVMDFCDGgDMNEYLLSRKPN----RKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd07861   72 -----NRLYL-----------------------VFEFLSM-DLKKYLDSLPKGkymdAELVKSYLYQILQGILFCHSRRV 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsASGQnpeePVSVnkcfLSTACGTDFYMAPEVWEG--HYTAKA 238
Cdd:cd07861  123 LHRDLKPQNLLI--------DNKGVIKLADFGLAR---AFGI----PVRV----YTHEVVTLWYRAPEVLLGspRYSTPV 183
                        250
                 ....*....|....*
gi 119628251 239 DIFALGIIIWAMLER 253
Cdd:cd07861  184 DIWSIGTIFAEMATK 198
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-251 1.38e-20

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 90.27  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHApeNVELALREFWALSSIksQHPNVIHLEEcILQKDgmvqkmshg 87
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV--DKKIVRTEIGVLLRL--SHPNIIKLKE-IFETP--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQLVEtslKGEIaFDP--RSAYYlwfvmdfcdggdmneyllsrkpNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd14085   71 TEISLVLELVT---GGEL-FDRivEKGYY----------------------SERDAADAVKQILEAVAYLHENGIVHRDL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLDTSdleptLKVADFGLSKVCsasgqnpEEPVSvnkcfLSTACGTDFYMAPEVWEG-HYTAKADIFALG 244
Cdd:cd14085  125 KPENLLYATPAPDAP-----LKIADFGLSKIV-------DQQVT-----MKTVCGTPGYCAPEILRGcAYGPEVDMWSVG 187

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd14085  188 VITYILL 194
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
7-251 1.59e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 89.67  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVA---VKKIRCHAPENveLALREFWALSSIKsqHPNVIHLEEcilqkdgmvqk 83
Cdd:cd14183    7 RYKVGRTIGDGNFAVVKECVERSTGREYAlkiINKSKCRGKEH--MIQNEVSILRRVK--HPNIVLLIE----------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvETSLKGEiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIH 162
Cdd:cd14183   72 --------------EMDMPTE----------LYLVMELVKGGDLFDAITSTNKYTERDASGMLyNLASAIKYLHSLNIVH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsDLEPTLKVADFGLSKVCSASgqnpeepvsvnkcfLSTACGTDFYMAPE-VWEGHYTAKADIF 241
Cdd:cd14183  128 RDIKPENLLVYEHQ----DGSKSLKLGDFGLATVVDGP--------------LYTVCGTPTYVAPEiIAETGYGLKVDIW 189
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14183  190 AAGVITYILL 199
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
12-250 1.65e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 89.28  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN--VELALREFWALSSIKsqHPNV-------IHLEECILqkdgmvq 82
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPktIKEIADEMKVLEGLD--HPNLvryygveVHREEVYI------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetslkgeiafdprsayylwFvMDFCDGGDMNEYL-LSRKPNRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd06626   77 ----------------------------------F-MEYCQEGTLEELLrHGRILDEAVIRVYTLQLLEGLAYLHENGIV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILisqtrLDTSDLeptLKVADFGLSKVcSASGQNPEEPVSVNkcflsTACGTDFYMAPEV-----WEGHYTA 236
Cdd:cd06626  122 HRDIKPANIF-----LDSNGL---IKLGDFGSAVK-LKNNTTTMAPGEVN-----SLVGTPAYMAPEVitgnkGEGHGRA 187
                        250
                 ....*....|....
gi 119628251 237 kADIFALGIIIWAM 250
Cdd:cd06626  188 -ADIWSLGCVVLEM 200
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
8-252 2.33e-20

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 89.32  E-value: 2.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSikSQHPNVIHLEEcilqkdgmvqkmshg 87
Cdd:cd06643    7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILAS--CDHPNIVKLLD--------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiAFdprsaYY---LWFVMDFCDGGDMNEYLLS-RKPNRKTNTSFML-QLSSALAFLHKNQIIH 162
Cdd:cd06643   70 ------------------AF-----YYennLWILIEFCAGGAVDAVMLElERPLTEPQIRVVCkQTLEALVYLHENKIIH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISqtrldtsdLEPTLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPEVW------EGHYTA 236
Cdd:cd06643  127 RDLKAGNILFT--------LDGDIKLADFGVSAKNTRTLQRRDSFI-----------GTPYWMAPEVVmcetskDRPYDY 187
                        250
                 ....*....|....*.
gi 119628251 237 KADIFALGIIIWAMLE 252
Cdd:cd06643  188 KADVWSLGVTLIEMAQ 203
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
11-253 2.38e-20

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 89.71  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL---ALREFWALSSIKsqHPNVIHLEECILQKdgmvqkmshg 87
Cdd:cd06633   26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqdIIKEVKFLQQLK--HPNTIEYKGCYLKD---------- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLS-SALAFLHKNQIIHRDLK 166
Cdd:cd06633   94 -------------------------HTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGAlQGLAYLHSHNMIHRDIK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISqtrldtsdlEP-TLKVADFGlskvcSASGQNPEepvsvnkcflSTACGTDFYMAPEVW----EGHYTAKADIF 241
Cdd:cd06633  149 AGNILLT---------EPgQVKLADFG-----SASIASPA----------NSFVGTPYWMAPEVIlamdEGQYDGKVDIW 204
                        250
                 ....*....|..
gi 119628251 242 ALGIIIWAMLER 253
Cdd:cd06633  205 SLGITCIELAER 216
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
8-332 2.40e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 89.46  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENV-ELALREFWALSSIKsqHPNVIHLEECILQKDGMVqkmsh 86
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTpSTAIREISLMKELK--HENIVRLHDVIHTENKLM----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayylwFVMDFCDGgDMNEYLLSR------KPNrkTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd07836   75 ------------------------------LVFEYMDK-DLKKYMDTHgvrgalDPN--TVKSFTYQLLKGIAFCHENRV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKvcsASGqnpeepVSVNKcfLSTACGTDFYMAPEVWEGH--YTAKA 238
Cdd:cd07836  122 LHRDLKPQNLLINK--------RGELKLADFGLAR---AFG------IPVNT--FSNEVVTLWYRAPDVLLGSrtYSTSI 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIiwaMLERIT----FIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSmngRMKQLIkemlaa 314
Cdd:cd07836  183 DIWSVGCI---MAEMITgrplFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEYKPTFPRYPPQ---DLQQLF------ 250
                        330
                 ....*....|....*...
gi 119628251 315 nPQDRPDAFELELRLVQI 332
Cdd:cd07836  251 -PHADPLGIDLLHRLLQL 267
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
14-320 2.53e-20

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 88.66  E-value: 2.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAP---ENVELaLREFWALSsiKSQHPNVIhleeCILqkdGMVQKMSHgsns 90
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNcieERKAL-LKEAEKME--RARHSYVL----PLL---GVCVERRS---- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSF--MLQLSSALAFLH--KNQIIHRDLK 166
Cdd:cd13978   67 ------------------------LGLVMEYMENGSLKSLLEREIQDVPWSLRFriIHEIALGMNFLHnmDPPLLHHDLK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKcflstaCGTDFYMAPEVWEGHY---TAKADIFAL 243
Cdd:cd13978  123 PENILL--------DNHFHVKISDFGLSKLGMKSISANRRRGTENL------GGTPIYMAPEAFDDFNkkpTSKSDVYSF 188
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 244 GIIIWAMLERITFIDTETKKELLGSYVKQGteivpvgeallENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd13978  189 AIVIWAVLTRKEPFENAINPLLIMQIVSKG-----------DRPSLDDIGRLKQIENVQELISLMIRCWDGNPDARP 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
8-325 2.62e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 88.88  E-value: 2.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREV-GRGSYGVVYEAVIRKTSARVAVKKIR--CHAPENVELALRefwalssiKSQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14089    2 YTISKQVlGLGINGKVLECFHKKTGEKFALKVLRdnPKARREVELHWR--------ASGCPHIVRIID------------ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnssLYlqlvetslkgEIAFDPRSayYLWFVMDFCDGGDmneyLLSRKPNRkTNTSF--------MLQLSSALAFLH 156
Cdd:cd14089   62 -------VY----------ENTYQGRK--CLLVVMECMEGGE----LFSRIQER-ADSAFtereaaeiMRQIGSAVAHLH 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTRLDTsdlepTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEG-HYT 235
Cdd:cd14089  118 SMNIAHRDLKPENLLYSSKGPNA-----ILKLTDFGFAKETT------------TKKSLQTPCYTPYYVAPEVLGPeKYD 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAMleritfidtetkkeLLGS---YVKQGTEIvpvgealleNPKMellipvKKKSMNGR--------- 303
Cdd:cd14089  181 KSCDMWSLGVIMYIL--------------LCGYppfYSNHGLAI---------SPGM------KKRIRNGQyefpnpews 231
                        330       340
                 ....*....|....*....|....*..
gi 119628251 304 -----MKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14089  232 nvseeAKDLIRGLLKTDPSERLTIEEV 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
7-325 3.69e-20

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 88.59  E-value: 3.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIrevGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQ--------HPNVihleecilqkd 78
Cdd:cd06629    5 KGELI---GKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQKTVVDALKSEidtlkdldHPNI----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmVQkmshgsnsslYLQLVETSLkgeiafdprsayYLWFVMDFCDGGDMNEYLlsRKPNR---KTNTSFMLQLSSALAFL 155
Cdd:cd06629   71 --VQ----------YLGFEETED------------YFSIFLEYVPGGSIGSCL--RKYGKfeeDLVRFFTRQILDGLAYL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVcSASGQNPEEPVSVNkcflstacGTDFYMAPEV---WEG 232
Cdd:cd06629  125 HSKGILHRDLKADNILV--------DLEGICKISDFGISKK-SDDIYGNNGATSMQ--------GSVFWMAPEVihsQGQ 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 HYTAKADIFALGIIIWAML--ERitfidTETKKELLGSYVKQGTE--IVPVGEALLENPKMEllipvkkksmngrmkQLI 308
Cdd:cd06629  188 GYSAKVDIWSLGCVVLEMLagRR-----PWSDDEAIAAMFKLGNKrsAPPVPEDVNLSPEAL---------------DFL 247
                        330
                 ....*....|....*..
gi 119628251 309 KEMLAANPQDRPDAFEL 325
Cdd:cd06629  248 NACFAIDPRDRPTAAEL 264
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
7-305 3.81e-20

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 87.96  E-value: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVELALREFWALSSIksQHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIdkTQLNPSSLQKLFREVRIMKIL--NHPNIVKLFEVI---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLS--RKPNRKTNTSFMlQLSSALAFLHKNQIIH 162
Cdd:cd14072   69 --ETEKTLYL-----------------------VMEYASGGEVFDYLVAhgRMKEKEARAKFR-QIVSAVQYCHQKRIVH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSVNKcfLSTACGTDFYMAPEVWEG-HYTA-KADI 240
Cdd:cd14072  123 RDLKAENLLL--------DADMNIKIADFGFSN----------EFTPGNK--LDTFCGSPPYAAPELFQGkKYDGpEVDV 182
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLERITFIDTETKKELLgSYVKQGTEIVPV-----GEALLEnpKMELLIPVKKKSMNGRMK 305
Cdd:cd14072  183 WSLGVILYTLVSGSLPFDGQNLKELR-ERVLRGKYRIPFymstdCENLLK--KFLVLNPSKRGTLEQIMK 249
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
8-251 3.88e-20

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 88.63  E-value: 3.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREV-GRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREfwalssiksqhpnvihleecilqkdgmVQKMSH 86
Cdd:cd14090    3 YKLTGELlGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFRE---------------------------VETLHQ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDmneyLLSRKPNRKTNT----SFMLQ-LSSALAFLHKNQII 161
Cdd:cd14090   56 CQGHPNILQLIEY-------FEDDERFYL--VFEKMRGGP----LLSHIEKRVHFTeqeaSLVVRdIASALDFLHDKGIA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldTSDLEPtLKVADFGLSKVCSASGQNpEEPVSVNKcfLSTACGTDFYMAPEV-----WEGH-YT 235
Cdd:cd14090  123 HRDLKPENILCES----MDKVSP-VKICDFDLGSGIKLSSTS-MTPVTTPE--LLTPVGSAEYMAPEVvdafvGEALsYD 194
                        250
                 ....*....|....*.
gi 119628251 236 AKADIFALGIIIWAML 251
Cdd:cd14090  195 KRCDLWSLGVILYIML 210
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
8-255 6.21e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 88.53  E-value: 6.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRefwalssiKSQHPNVIHLEEciLQKDGMvqkm 84
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKiidKSKRDPSEEIEILLR--------YGQHPNIITLKD--VYDDGK---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd14178   71 -----------------------------FVYLVMELMRGGELLDRILRQKCFSEREASAVLcTITKTVEYLHSQGVVHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd14178  122 DLKPSNILY----MDESGNPESIRICDFGFAKQLRAENG-----------LLMTPCYTANFVAPEVLKRQgYDAACDIWS 186
                        250
                 ....*....|...
gi 119628251 243 LGIIIWAMLERIT 255
Cdd:cd14178  187 LGILLYTMLAGFT 199
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-329 7.83e-20

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 87.41  E-value: 7.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   9 DLIREVGRGSYGVVYEAVIRKTsaRVAVKKIRCHAPenvelALREFWALSSIKS--QHPNVIHLEECILQKDGmvqkmsh 86
Cdd:cd05039    9 KLGELIGKGEFGDVMLGDYRGQ--KVAVKCLKDDST-----AAQAFLAEASVMTtlRHPNLVQLLGVVLEGNG------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnssLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKP---NRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05039   75 -----LYI-----------------------VTEYMAKGSLVDYLRSRGRaviTRKDQLGFALDVCEGMEYLESKKFVHR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYTAKADIFA 242
Cdd:cd05039  127 DLAARNVLVSE--------DNVAKVSDFGLAKEASSNQDGGKLPIK--------------WTAPEaLREKKFSTKSDVWS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWamleritfidtetkkellgsyvkqgtEIVPVGEAllENPKMELLIPVKKKSMNGRMK----------QLIKEML 312
Cdd:cd05039  185 FGILLW--------------------------EIYSFGRV--PYPRIPLKDVVPHVEKGYRMEapegcppevyKVMKNCW 236
                        330
                 ....*....|....*..
gi 119628251 313 AANPQDRPDAFELELRL 329
Cdd:cd05039  237 ELDPAKRPTFKQLREKL 253
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
8-251 8.67e-20

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 87.31  E-value: 8.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKymnKQKCIEKDSVRNVLNELEILQEL--EHPFLVNLWY------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDPRSayYLWFVMDFCDGGDMnEYLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIH 162
Cdd:cd05578   68 ---------------------SFQDEE--DMYMVVDLLLGGDL-RYHLQQKVKFSEETVkfYICEIVLALDYLHSKNIIH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNpeepvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd05578  124 RDIKPDNILL--------DEQGHVHITDFNIATKLTDGTLA------------TSTSGTKPYMAPEVFMRAgYSFAVDWW 183
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd05578  184 SLGVTAYEML 193
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
7-323 1.11e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 87.78  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSAR-VAVKKIRCH-APENVELA-LREFWALSSIKS-QHPNVIHL-EECILQKDGMV 81
Cdd:cd07862    2 QYECVAEIGEGAYGKVFKARDLKNGGRfVALKRVRVQtGEEGMPLStIREVAVLRHLETfEHPNVVRLfDVCTVSRTDRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMShgsnsslylqlvetslkgeiafdprsayylwFVMDFCDGgDMNEYLlSRKPN----RKTNTSFMLQLSSALAFLHK 157
Cdd:cd07862   82 TKLT-------------------------------LVFEHVDQ-DLTTYL-DKVPEpgvpTETIKDMMFQLLRGLDFLHS 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSAsgqnpeepvsvnKCFLSTACGTDFYMAPEV-WEGHYTA 236
Cdd:cd07862  129 HRVVHRDLKPQNILVTSS--------GQIKLADFGLARIYSF------------QMALTSVVVTLWYRAPEVlLQSSYAT 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMLERITFIDTETKKELLGSYVK----QGTEIVPVGEALLENP-------KMELLIPvkkkSMNGRMK 305
Cdd:cd07862  189 PVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDviglPGEEDWPRDVALPRQAfhsksaqPIEKFVT----DIDELGK 264
                        330
                 ....*....|....*...
gi 119628251 306 QLIKEMLAANPQDRPDAF 323
Cdd:cd07862  265 DLLLKCLTFNPAKRISAY 282
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
3-251 1.26e-19

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 89.32  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   3 SSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapENVELALREFWALSSIksQHPNVIHLeecilqKDGMVQ 82
Cdd:PTZ00036  63 SPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVL----QDPQYKNRELLIMKNL--NHINIIFL------KDYYYT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVetslkgeIAFDPRSAYylwfvmdfcdggdmnEYLLSRKPNRKTNTSFML-----QLSSALAFLHK 157
Cdd:PTZ00036 131 ECFKKNEKNIFLNVV-------MEFIPQTVH---------------KYMKHYARNNHALPLFLVklysyQLCRALAYIHS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrldtsdlEP---TLKVADFGLSKVCSAsGQNPeepvsvnkcfLSTACgTDFYMAPEVWEG-- 232
Cdd:PTZ00036 189 KFICHRDLKPQNLLI----------DPnthTLKLCDFGSAKNLLA-GQRS----------VSYIC-SRFYRAPELMLGat 246
                        250
                 ....*....|....*....
gi 119628251 233 HYTAKADIFALGIIIWAML 251
Cdd:PTZ00036 247 NYTTHIDLWSLGCIIAEMI 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
7-250 1.37e-19

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 86.71  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSA---RVAVKKIRCH--APENVELALREFWALSSIksQHPNVIHLEECILQKDgmv 81
Cdd:cd08222    1 RYRVVRKLGSGNFGTVYLVSDLKATAdeeLKVLKEISVGelQPDETVDANREAKLLSKL--DHPAIVKFHDSFVEKE--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTS-----FMLQLSSALAFLH 156
Cdd:cd08222   76 --------------------------------SFCIVTEYCEGGDLDDKISEYKKSGTTIDEnqildWFIQLLLAVQYMH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTrldtsdlepTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YT 235
Cdd:cd08222  124 ERRILHRDLKAKNIFLKNN---------VIKVGDFGISRILMGTSD-----------LATTFTGTPYYMSPEVLKHEgYN 183
                        250
                 ....*....|....*
gi 119628251 236 AKADIFALGIIIWAM 250
Cdd:cd08222  184 SKSDIWSLGCILYEM 198
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
8-245 1.50e-19

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 87.36  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELAlREFWALSSIkSQHPNVIHLEecilqkdGMVQKMSHG 87
Cdd:cd06639   24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIE-AEYNILRSL-PNHPNVVKFY-------GMFYKADQY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSlylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYL--LSRKPNRKTNTSFMLQLSSA---LAFLHKNQIIH 162
Cdd:cd06639   95 VGGQ-----------------------LWLVLELCNGGSVTELVkgLLKCGQRLDEAMISYILYGAllgLQHLHNNRIIH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnKCFLSTACGTDFYMAPEV------WEGHYTA 236
Cdd:cd06639  152 RDVKGNNILLTT--------EGGVKLVDFGVSAQLTSA-----------RLRRNTSVGTPFWMAPEViaceqqYDYSYDA 212

                 ....*....
gi 119628251 237 KADIFALGI 245
Cdd:cd06639  213 RCDVWSLGI 221
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
6-251 1.61e-19

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 87.75  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrchAPENVEL----ALREFWALSSIKsqHPNVIHLEEciLQKDGMV 81
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI---SPFEHQTyclrTLREIKILLRFK--HENIIGILD--IQRPPTF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMShgsnsSLYL--QLVETSLKGEIAFDPRSayylwfvmdfcdgGDMNEYllsrkpnrktntsFMLQLSSALAFLHKNQ 159
Cdd:cd07849   78 ESFK-----DVYIvqELMETDLYKLIKTQHLS-------------NDHIQY-------------FLYQILRGLKYIHSAN 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQtrldTSDleptLKVADFGLSKVCSasgqnpeePVSVNKCFLSTACGTDFYMAPEVW--EGHYTAK 237
Cdd:cd07849  127 VLHRDLKPSNLLLNT----NCD----LKICDFGLARIAD--------PEHDHTGFLTEYVATRWYRAPEIMlnSKGYTKA 190
                        250
                 ....*....|....
gi 119628251 238 ADIFALGIIIWAML 251
Cdd:cd07849  191 IDIWSVGCILAEML 204
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
108-325 1.71e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 88.92  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 108 DPRSAYYLWFVMDFCDGGDMN----EYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdl 182
Cdd:PTZ00267 133 DFKSDDKLLLIMEYGSGGDLNkqikQRLKEHLPFQEYEVGLLFyQIVLALDEVHSRKMMHRDLKSANIFLMPTGI----- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 183 eptLKVADFGLSKVCSASgqnpeepVSVNkcFLSTACGTDFYMAPEVWE-GHYTAKADIFALGIIIWAMLERITFIDTET 261
Cdd:PTZ00267 208 ---IKLGDFGFSKQYSDS-------VSLD--VASSFCGTPYYLAPELWErKRYSKKADMWSLGVILYELLTLHRPFKGPS 275
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 262 KKELLGSYVKQGTEIVPVGeallenpkmellipvkkksMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:PTZ00267 276 QREIMQQVLYGKYDPFPCP-------------------VSSGMKALLDPLLSKNPALRPTTQQL 320
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
7-253 1.75e-19

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 87.81  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALRefwALSSIK----SQHPNVIHLEECILQkdgmVQ 82
Cdd:cd07858    6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIA-NAFDNRIDAKR---TLREIKllrhLDHENVIAIKDIMPP----PH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHgsnSSLYL--QLVETSLKGEIafdpRSAYYLwfVMDFCdggdmnEYllsrkpnrktntsFMLQLSSALAFLHKNQI 160
Cdd:cd07858   78 REAF---NDVYIvyELMDTDLHQII----RSSQTL--SDDHC------QY-------------FLYQLLRGLKYIHSANV 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISqTRLDtsdleptLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEV---WEGhYTAK 237
Cdd:cd07858  130 LHRDLKPSNLLLN-ANCD-------LKICDFGLARTTSEKGD-----------FMTEYVVTRWYRAPELllnCSE-YTTA 189
                        250
                 ....*....|....*.
gi 119628251 238 ADIFALGIIIWAMLER 253
Cdd:cd07858  190 IDVWSVGCIFAELLGR 205
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
8-251 2.19e-19

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 86.67  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL-ALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkmsH 86
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFtAIREASLLKDLK--HANIVTLHDII-----------H 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNS-SLYLQLVETSLKgeiafdprsAYylwfvMDFCDGG-DMNEYLLsrkpnrktntsFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd07844   69 TKKTlTLVFEYLDTDLK---------QY-----MDDCGGGlSMHNVRL-----------FLFQLLRGLAYCHQRRVLHRD 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKADIFA 242
Cdd:cd07844  124 LKPQNLLISER--------GELKLADFGLARAKSVPSKTYSNEVV-----------TLWYRPPDVLLGstEYSTSLDMWG 184

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd07844  185 VGCIFYEMA 193
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-251 3.00e-19

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 86.10  E-value: 3.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALR-EFWALSSIksQHPNVIHLEEcilqkdgmvqkmSH 86
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVEnEIAVLRRI--NHENIVSLED------------IY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDL 165
Cdd:cd14169   71 ESPTHLYL-----------------------AMELVTGGELFDRIIERGSYTEKDASQLIgQVLQAVKYLHQLGIVHRDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNiLISQTRLDTSdlepTLKVADFGLSKVcSASGqnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTAKA-DIFALG 244
Cdd:cd14169  128 KPEN-LLYATPFEDS----KIMISDFGLSKI-EAQG------------MLSTACGTPGYVAPELLEQKPYGKAvDVWAIG 189

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd14169  190 VISYILL 196
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
7-251 3.20e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 86.18  E-value: 3.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREfwalssIKSQHPNVIHLeecilqkdgmvqkMSH 86
Cdd:cd14181   11 KYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLEE------VRSSTLKEIHI-------------LRQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLQLVETSlkgeiafdpRSAYYLWFVMDFCDGGDMNEYL-----LSRKPNRktntSFMLQLSSALAFLHKNQII 161
Cdd:cd14181   72 VSGHPSIITLIDSY---------ESSTFIFLVFDLMRRGELFDYLtekvtLSEKETR----SIMRSLLEAVSYLHANNIV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILIsqtrldtsDLEPTLKVADFGLSkvCSASgqnPEEPvsvnkcfLSTACGTDFYMAPEVW-----EGH--Y 234
Cdd:cd14181  139 HRDLKPENILL--------DDQLHIKLSDFGFS--CHLE---PGEK-------LRELCGTPGYLAPEILkcsmdETHpgY 198
                        250
                 ....*....|....*..
gi 119628251 235 TAKADIFALGIIIWAML 251
Cdd:cd14181  199 GKEVDLWACGVILFTLL 215
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
7-324 3.42e-19

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 86.96  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchAP-ENVELALREFWALSSIKS-QHPNVIHLEECilqkdgmvqkm 84
Cdd:cd07851   16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLS--RPfQSAIHAKRTYRELRLLKHmKHENVIGLLDV----------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiaFDPRSAyylwfVMDFCD--------GGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH 156
Cdd:cd07851   83 ----------------------FTPASS-----LEDFQDvylvthlmGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIH 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILIsqtrldTSDLEptLKVADFGLSKVCSASgqnpeepvsvnkcfLSTACGTDFYMAPEV--WEGHY 234
Cdd:cd07851  136 SAGIIHRDLKPSNLAV------NEDCE--LKILDFGLARHTDDE--------------MTGYVATRWYRAPEImlNWMHY 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 TAKADIFALGIIIWAMLeritfidteTKKELL-GS-YVKQGTEIVPV----GEALLENPKMELL------IPVKKKS--- 299
Cdd:cd07851  194 NQTVDIWSVGCIMAELL---------TGKTLFpGSdHIDQLKRIMNLvgtpDEELLKKISSESArnyiqsLPQMPKKdfk 264
                        330       340       350
                 ....*....|....*....|....*....|
gi 119628251 300 -----MNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd07851  265 evfsgANPLAIDLLEKMLVLDPDKRITAAE 294
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
12-265 3.43e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 86.88  E-value: 3.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSsIKSQHPNVIHLEECILQKDgmvqkmshgs 88
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVilqDDDVECTMTEKRILS-LARNHPFLTQLYCCFQTPD---------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslylqlvetslkgeiafdprsayYLWFVMDFCDGGD-MNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd05590   70 -------------------------RLFFVMEFVNGGDlMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSvNKCFLSTACGTDFYMAPEVW-EGHYTAKADIFALGII 246
Cdd:cd05590  125 DNVLL--------DHEGHCKLADFGMCK----------EGIF-NGKTTSTFCGTPDYIAPEILqEMLYGPSVDWWAMGVL 185
                        250
                 ....*....|....*....
gi 119628251 247 IWAMLERITFIDTETKKEL 265
Cdd:cd05590  186 LYEMLCGHAPFEAENEDDL 204
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
8-322 3.63e-19

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 85.38  E-value: 3.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPEN-VELALREFWALSsiksqHPNVIHLEEcilqkdgmvqk 83
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKiidKSKLKGKEDmIESEILIIKSLS-----HPNIVKLFE----------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqLVETSLKgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIH 162
Cdd:cd14185   66 ------------VYETEKE------------IYLILEYVRGGDLFDAIIESVKFTEHDAALMIiDLCEALVYIHSKHIVH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldTSDLEPTLKVADFGLSKVCSASgqnpeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd14185  122 RDLKPENLLVQH----NPDKSTTLKLADFGLAKYVTGP--------------IFTVCGTPTYVAPEILSEKgYGLEVDMW 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERI-TFIDTETKKELLgsyvkqgTEIVPVGEallenpkMELLIPVkKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14185  184 AAGVILYILLCGFpPFRSPERDQEEL-------FQIIQLGH-------YEFLPPY-WDNISEAAKDLISRLLVVDPEKRY 248

                 ..
gi 119628251 321 DA 322
Cdd:cd14185  249 TA 250
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
11-322 4.90e-19

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 85.78  E-value: 4.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL-ALREFWALSSIKsqHPNVIHLEECILQKDGMvqkmshgsn 89
Cdd:cd07870    5 LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFtAIREASLLKGLK--HANIVLLHDIIHTKETL--------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sSLYLQLVETSLKGEIAFDPrsayylwfvmdfcdgGDMNEYLLSRkpnrktntsFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd07870   74 -TFVFEYMHTDLAQYMIQHP---------------GGLHPYNVRL---------FMFQLLRGLAYIHGQHILHRDLKPQN 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISQTrldtsdlePTLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFALGIII 247
Cdd:cd07870  129 LLISYL--------GELKLADFGLARAKSIPSQT-----------YSSEVVTLWYRPPDVLLGatDYSSALDIWGAGCIF 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 248 WAMLE-RITFIDTETKKE-LLGSYVKQG--TEIVPVGEALLENPKMELLIPVKKKSMN---GRMKQ------LIKEMLAA 314
Cdd:cd07870  190 IEMLQgQPAFPGVSDVFEqLEKIWTVLGvpTEDTWPGVSKLPNYKPEWFLPCKPQQLRvvwKRLSRppkaedLASQMLMM 269

                 ....*...
gi 119628251 315 NPQDRPDA 322
Cdd:cd07870  270 FPKDRISA 277
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
9-247 6.04e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 85.09  E-value: 6.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   9 DLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapenvelalrefwalSSIKSQHPNVIHLEECILQKdgmvqkmshgS 88
Cdd:cd06605    4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIR-----------------LEIDEALQKQILRELDVLHK----------C 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETSL-KGEIafdprsayylWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-LQLSSALAFLH-KNQIIHRDL 165
Cdd:cd06605   57 NSPYIVGFYGAFYsEGDI----------SICMEYMDGGSLDKILKEVGRIPERILGKIaVAVVKGLIYLHeKHKIIHRDV 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNpeepvsvnkcflsTACGTDFYMAPEVWEG-HYTAKADIFALG 244
Cdd:cd06605  127 KPSNILVNS--------RGQVKLCDFGVSGQLVDSLAK-------------TFVGTRSYMAPERISGgKYTVKSDIWSLG 185

                 ...
gi 119628251 245 III 247
Cdd:cd06605  186 LSL 188
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-251 6.99e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 85.69  E-value: 6.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElalREFWALSSIKSqHPNVIHLEECILQKdgmvqkmshgsnssly 93
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ---REVAALRLCQS-HPNIVALHEVLHDQ---------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14180   74 -------------------YHTYLVMELLRGGELLDRIKKKARFSESEASqLMRSLVSAVSFMHEAGVVHRDLKPENILY 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SqtrlDTSDLEPtLKVADFGLSKVCSAsgqnPEEPvsvnkcfLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAML 251
Cdd:cd14180  135 A----DESDGAV-LKVIDFGFARLRPQ----GSRP-------LQTPCFTLQYAAPELFsNQGYDESCDLWSLGVILYTML 198
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
7-322 7.36e-19

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 85.17  E-value: 7.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARV-AVKKIRCHA--PENVELALREFWALSSIKSQ-HPNVIHLEEcilqkdgmvq 82
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYagAKDRLRRLEEVSILRELTLDgHDNIVQLID---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmSHGSNSSLYLQLvetslkgeiafdprsayylwfvmDFCDGGDMNEYL-----LSRKPNRKTNTSfMLQLSSALAFLHK 157
Cdd:cd14052   71 --SWEYHGHLYIQT-----------------------ELCENGSLDVFLselglLGRLDEFRVWKI-LVELSLGLRFIHD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDFYMAPEVWEGH-YTA 236
Cdd:cd14052  125 HHFVHLDLKPANVLITF--------EGTLKIGDFGMATVWPLIRGIERE-------------GDREYIAPEILSEHmYDK 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIII---------------WAMLERITFIDTET-KKELLGSYVKQGTEIVPVgeallenpkmelliPVKKKSM 300
Cdd:cd14052  184 PADIFSLGLILleaaanvvlpdngdaWQKLRSGDLSDAPRlSSTDLHSASSPSSNPPPD--------------PPNMPIL 249
                        330       340
                 ....*....|....*....|..
gi 119628251 301 NGRMKQLIKEMLAANPQDRPDA 322
Cdd:cd14052  250 SGSLDRVVRWMLSPEPDRRPTA 271
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
11-253 7.58e-19

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 85.87  E-value: 7.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL---ALREFWALSSIKsqHPNVIHLEECILQKdgmvqkmshg 87
Cdd:cd06635   30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqdIIKEVKFLQRIK--HPNSIEYKGCYLRE---------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLS-SALAFLHKNQIIHRDLK 166
Cdd:cd06635   98 -------------------------HTAWLVMEYCLGSASDLLEVHKKPLQEIEIAAITHGAlQGLAYLHSHNMIHRDIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISqtrldtsdlEP-TLKVADFGlskvcSASGQNPEepvsvnkcflSTACGTDFYMAPEVW----EGHYTAKADIF 241
Cdd:cd06635  153 AGNILLT---------EPgQVKLADFG-----SASIASPA----------NSFVGTPYWMAPEVIlamdEGQYDGKVDVW 208
                        250
                 ....*....|..
gi 119628251 242 ALGIIIWAMLER 253
Cdd:cd06635  209 SLGITCIELAER 220
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
8-325 8.79e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 84.86  E-value: 8.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARV-AVKKIRCHAP------ENVELALREFWA-LSSIKSQ--HPNVIHLEECILQK 77
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNPafgrteQERDKSVGDIISeVNIIKEQlrHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  78 DgmvqkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRK------PNRKTNTSFMlQLSSA 151
Cdd:cd08528   82 D-----------------------------------RLYIVMELIEGAPLGEHFSSLKeknehfTEDRIWNIFV-QMVLA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 152 LAFLHK-NQIIHRDLKPDNILISQTRLDTsdleptlkVADFGLSKvcsasgQNPEEpvsvnKCFLSTACGTDFYMAPEVW 230
Cdd:cd08528  126 LRYLHKeKQIVHRDLKPNNIMLGEDDKVT--------ITDFGLAK------QKGPE-----SSKMTSVVGTILYSCPEIV 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 231 EGH-YTAKADIFALGIIIWAMLERITFIDTETKKELlgsyvkqGTEIVpvgEALLEnpkmelliPVKKKSMNGRMKQLIK 309
Cdd:cd08528  187 QNEpYGEKADIWALGCILYQMCTLQPPFYSTNMLTL-------ATKIV---EAEYE--------PLPEGMYSDDITFVIR 248
                        330
                 ....*....|....*.
gi 119628251 310 EMLAANPQDRPDAFEL 325
Cdd:cd08528  249 SCLTPDPEARPDIVEV 264
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
7-251 9.03e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 85.43  E-value: 9.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREV---GRGSYGVVYEAVIRKTSARVAVKKI--RCHApenvelaLREFWALSSIKSqHPNVIHLEEcILQkdgmv 81
Cdd:cd14092    4 NYELDLREealGDGSFSVCRKCVHKKTGQEFAVKIVsrRLDT-------SREVQLLRLCQG-HPNIVKLHE-VFQ----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafDPRSAYylwFVMDFCDGGDmneyLLSRKPNRKTNT-----SFMLQLSSALAFLH 156
Cdd:cd14092   70 --------------------------DELHTY---LVMELLRGGE----LLERIRKKKRFTeseasRIMRQLVSAVSFMH 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQtrlDTSDLEptLKVADFGLSKVcsasgqNPEEPVsvnkcfLSTACGTDFYMAPEV-----WE 231
Cdd:cd14092  117 SKGVVHRDLKPENLLFTD---EDDDAE--IKIVDFGFARL------KPENQP------LKTPCFTLPYAAPEVlkqalST 179
                        250       260
                 ....*....|....*....|
gi 119628251 232 GHYTAKADIFALGIIIWAML 251
Cdd:cd14092  180 QGYDESCDLWSLGVILYTML 199
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
7-325 1.02e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 84.78  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrCHAPENVE---LALREFWALSSIKsqHPNVIHLEECILQKdgmvqk 83
Cdd:cd07846    2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKF-LESEDDKMvkkIAMREIKMLKQLR--HENLVNLIEVFRRK------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEylLSRKPN---RKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd07846   73 ------KRWYL-----------------------VFEFVDHTVLDD--LEKYPNgldESRVRKYLFQILRGIDFCHSHNI 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKA 238
Cdd:cd07846  122 IHRDIKPENILVSQSGV--------VKLCDFGFARTLAAPGEVYTDYVA-----------TRWYRAPELLVGdtKYGKAV 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAMLERITFIDTETKKELLGSYVK-QGTEIVPVGEALLEN--------PKMELLIPVKKK--SMNGRMKQL 307
Cdd:cd07846  183 DVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKcLGNLIPRHQELFQKNplfagvrlPEVKEVEPLERRypKLSGVVIDL 262
                        330
                 ....*....|....*...
gi 119628251 308 IKEMLAANPQDRPDAFEL 325
Cdd:cd07846  263 AKKCLHIDPDKRPSCSEL 280
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7-251 1.03e-18

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 84.27  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC--HAPENVElalREFWALSSIKsqHPNVIHLEECILQKDGMVQKM 84
Cdd:cd14665    1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERgeKIDENVQ---REIINHRSLR--HPNIVRFKEVILTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLQLvetslkgeiafdprsayylwfvmdfCDGGDMNEyllsrkpnrKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14665   76 EYAAGGELFERI-------------------------CNAGRFSE---------DEARFFFQQLISGVSYCHSMQICHRD 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILisqtrLDTSDlEPTLKVADFGLSKVCSASGQnPEEPVsvnkcflstacGTDFYMAPEVW-EGHYTAK-ADIFA 242
Cdd:cd14665  122 LKLENTL-----LDGSP-APRLKICDFGYSKSSVLHSQ-PKSTV-----------GTPAYIAPEVLlKKEYDGKiADVWS 183

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd14665  184 CGVTLYVML 192
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-319 1.14e-18

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 84.98  E-value: 1.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPEN-VELALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd05574    3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLdkEEMIKRNkVKRVLTEREILATLD--HPFLPTLYASF---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdpRSAYYLWFVMDFCDGGDMNEyLLSRKPNRktntsfMLQLSS----------ALAF 154
Cdd:cd05574   71 -------------------------QTSTHLCFVMDYCPGGELFR-LLQKQPGK------RLPEEVarfyaaevllALEY 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILISQ------TRLD---TSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTAC-GTDFY 224
Cdd:cd05574  119 LHLLGFVYRDLKPENILLHEsghimlTDFDlskQSSVTPPPVRKSLRKGSRRSSVKSIEKETFVAEPSARSNSFvGTEEY 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 225 MAPEVWEGH-YTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQgteivpvgeallenpkmELLIPvKKKSMNGR 303
Cdd:cd05574  199 IAPEVIKGDgHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKK-----------------ELTFP-ESPPVSSE 260
                        330
                 ....*....|....*.
gi 119628251 304 MKQLIKEMLAANPQDR 319
Cdd:cd05574  261 AKDLIRKLLVKDPSKR 276
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
14-251 1.15e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 85.24  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSsIKSQHPNVIHLEECILQKDgmvqkmshgsns 90
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVilqDDDVDCTMTEKRILA-LAAKHPFLTALHSCFQTKD------------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayYLWFVMDFCDGGD-MNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd05591   70 -----------------------RLFFVMEYVNGGDlMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDN 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNPeepvsvnkcflSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIW 248
Cdd:cd05591  127 ILL--------DAEGHCKLADFGMCKEGILNGKTT-----------TTFCGTPDYIAPEILqELEYGPSVDWWALGVLMY 187

                 ...
gi 119628251 249 AML 251
Cdd:cd05591  188 EMM 190
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-319 1.20e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 85.09  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElalREFWALSSIKSqHPNVIHLEEcilqkdgmvqkmshgsnssLY 93
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ---REIAALKLCEG-HPNIVKLHE-------------------VY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVETSLkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14179   72 HDQLHTFL----------------VMELLKGGELLERIKKKQHFSETEASHiMRKLVSAVSHMHDVGVVHRDLKPENLLF 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SqtrlDTSDlEPTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAML 251
Cdd:cd14179  136 T----DESD-NSEIKIIDFGFARLKPPDNQ-----------PLKTPCFTLHYAAPELLnYNGYDESCDLWSLGVILYTML 199
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 252 E-RITFIDTE-----TKKELLGSYVKQGtEIVPVGEALlenpkmellipvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14179  200 SgQVPFQCHDksltcTSAEEIMKKIKQG-DFSFEGEAW--------------KNVSQEAKDLIQGLLTVDPNKR 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
113-251 1.22e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 86.77  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 113 YYLwfVMDFCDGGDMNEYLLSRKP--NRKTnTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVAD 190
Cdd:NF033483  82 PYI--VMEYVDGRTLKDYIREHGPlsPEEA-VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDG--------RVKVTD 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 191 FGLSKVCSASG--QNpeepvsvnkcflSTACGTDFYMAPEVWEGHY-TAKADIFALGIIIWAML 251
Cdd:NF033483 151 FGIARALSSTTmtQT------------NSVLGTVHYLSPEQARGGTvDARSDIYSLGIVLYEML 202
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
14-251 1.26e-18

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 84.00  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKI-RCHAPENVELALR-EFWALSSIKsqHPNVIHLEecilqkdgmvqkmshgsnss 91
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVIdKLRFPTKQESQLRnEVAILQQLS--HPGVVNLE-------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylQLVETSLKgeiafdprsayyLWFVMDFCDGgDMNEYLLS----RKPNRktNTSFML-QLSSALAFLHKNQIIHRDLK 166
Cdd:cd14082   69 ---CMFETPER------------VFVVMEKLHG-DMLEMILSsekgRLPER--ITKFLVtQILVALRYLHSKNIVHCDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISqtrldTSDLEPTLKVADFGLSKVCSasgqnpeepvsvNKCFLSTACGTDFYMAPEVWEGH-YTAKADIFALGI 245
Cdd:cd14082  131 PENVLLA-----SAEPFPQVKLCDFGFARIIG------------EKSFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGV 193

                 ....*.
gi 119628251 246 IIWAML 251
Cdd:cd14082  194 IIYVSL 199
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
7-250 1.29e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 83.85  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKkirchapenvELALREFWALSSIKSQhpnvihlEECILqkdgmVQKMSH 86
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIK----------EIDLTKMPVKEKEASK-------KEVIL-----LAKMKH 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLQLVETSlkgeiafdprsayYLWFVMDFCDGGDmneylLSRKPNRKTNTSF--------MLQLSSALAFLHKN 158
Cdd:cd08225   59 PNIVTFFASFQENG-------------RLFIVMEYCDGGD-----LMKRINRQRGVLFsedqilswFVQISLGLKHIHDR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQTRLdtsdlepTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAK 237
Cdd:cd08225  121 KILHRDIKSQNIFLSKNGM-------VAKLGDFGIARQLNDSME-----------LAYTCVGTPYYLSPEICQNRpYNNK 182
                        250
                 ....*....|...
gi 119628251 238 ADIFALGIIIWAM 250
Cdd:cd08225  183 TDIWSLGCVLYEL 195
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
14-321 1.35e-18

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 83.98  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIRcHAP--------ENVELALREFWALSsiksqHPNVIHLEECILQKdgmvqkms 85
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKAAR-QDPdedisvtlENVRQEARLFWMLR-----HPNIIALRGVCLQP-------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafdPRsayyLWFVMDFCDGGDMNEYLLSRK--PNRKTNtsFMLQLSSALAFLHKNQ---I 160
Cdd:cd14061   66 -----------------------PN----LCLVMEYARGGALNRVLAGRKipPHVLVD--WAIQIARGMNYLHNEApvpI 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRLDTSDLEPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTACGTDFYMAPEVWEGHYTAKA-D 239
Cdd:cd14061  117 IHRDLKSSNILILEAIENEDLENKTLKITDFGLAR-------------EWHKTTRMSAAGTYAWMAPEVIKSSTFSKAsD 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLEritfidtetkkellGSYVKQGTEIVPVGEALLENpKMELLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14061  184 VWSYGVLLWELLT--------------GEVPYKGIDGLAVAYGVAVN-KLTLPIP---STCPEPFAQLMKDCWQPDPHDR 245

                 ..
gi 119628251 320 PD 321
Cdd:cd14061  246 PS 247
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
8-325 1.45e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 83.63  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGvvyEAVI-RKT--SARVAVKKIRCH-APENVEL-ALREFWALSsiksqhpnvihleecILQKDGMVQ 82
Cdd:cd08221    2 YIPVRVLGRGAFG---EAVLyRKTedNSLVVWKEVNLSrLSEKERRdALNEIDILS---------------LLNHDNIIT 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHG-SNSSLYLQlvetslkgeiafdprsayylwfvMDFCDGGDMNEYLLSRKPN---RKTNTSFMLQLSSALAFLHKN 158
Cdd:cd08221   64 YYNHFlDGESLFIE-----------------------MEYCNGGNLHDKIAQQKNQlfpEEVVLWYLYQIVSAVSHIHKA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEepvsvnkcflsTACGTDFYMAPEVWEG-HYTAK 237
Cdd:cd08221  121 GILHRDIKTLNIFLTKADL--------VKLGDFGISKVLDSESSMAE-----------SIVGTPYYMSPELVQGvKYNFK 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAMLERITFIDTETKKELLGSYVKqgteivpvGEALLENPKMELlipvkkksmngRMKQLIKEMLAANPQ 317
Cdd:cd08221  182 SDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ--------GEYEDIDEQYSE-----------EIIQLVHDCLHQDPE 242

                 ....*...
gi 119628251 318 DRPDAFEL 325
Cdd:cd08221  243 DRPTAEEL 250
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-251 1.53e-18

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 84.41  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKirchapenveLALREFWALSSIksQHpnvIHLEECILQKdgmvqkMSHG 87
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKV----------MAIPEVIRLKQE--QH---VHNEKRVLKE------VSHP 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYlqlvetslkgeiaFDPRSAYYLWFVMDFCDGGDMNEYLL-SRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd05612   62 FIIRLF-------------WTEHDQRFLYMLMEYVPGGELFSYLRnSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSKVCsasgqnpeepvsVNKCFlsTACGTDFYMAPEVWE--GHYTAkADIFALG 244
Cdd:cd05612  129 PENILL--------DKEGHIKLTDFGFAKKL------------RDRTW--TLCGTPEYLAPEVIQskGHNKA-VDWWALG 185

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd05612  186 ILIYEML 192
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
8-324 1.98e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 84.76  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEA--VIRKTSARVAVKKIrchapENV-------ELALREFWALSSIKSqHPNVIHLEECILQKD 78
Cdd:cd07857    2 YELIKELGQGAYGIVCSArnAETSEEETVAIKKI-----TNVfskkilaKRALRELKLLRHFRG-HKNITCLYDMDIVFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 GMVQKMShgsnssLYLQLVETslkgeiafdprsayylwfvmdfcdggDMNEYLLSRKPNRKTN-TSFMLQLSSALAFLHK 157
Cdd:cd07857   76 GNFNELY------LYEELMEA--------------------------DLHQIIRSGQPLTDAHfQSFIYQILCGLKYIHS 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrldTSDLEptLKVADFGLSKVCSAsgqNPEEpvsvNKCFLSTACGTDFYMAPEVWEGH--YT 235
Cdd:cd07857  124 ANVLHRDLKPGNLLV------NADCE--LKICDFGLARGFSE---NPGE----NAGFMTEYVATRWYRAPEIMLSFqsYT 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAMLERITFIDTEtkkellgSYVKQGTEIVPVgealLENPKMELLIPVKKKSMNGRMKQ--------- 306
Cdd:cd07857  189 KAIDVWSVGCILAELLGRKPVFKGK-------DYVDQLNQILQV----LGTPDEETLSRIGSPKAQNYIRSlpnipkkpf 257
                        330       340       350
                 ....*....|....*....|....*....|....
gi 119628251 307 -------------LIKEMLAANPQDR---PDAFE 324
Cdd:cd07857  258 esifpnanplaldLLEKLLAFDPTKRisvEEALE 291
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
108-330 2.11e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 85.69  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 108 DPRSAYYLWFVMDFCDGGDMNEYLLSRKpnrKTNTSF--------MLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdt 179
Cdd:PTZ00283 107 NPENVLMIALVLDYANAGDLRQEIKSRA---KTNRTFreheagllFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGL-- 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 180 sdleptLKVADFGLSKVCSASgqnpeepVS--VNKCFlstaCGTDFYMAPEVWEGH-YTAKADIFALGIIIWAMLERITF 256
Cdd:PTZ00283 182 ------VKLGDFGFSKMYAAT-------VSddVGRTF----CGTPYYVAPEIWRRKpYSKKADMFSLGVLLYELLTLKRP 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 257 IDTETKKE-----LLGSYVKQGTEIVP-----VGEALLENPKMElliPVKKKSMNGRMKQLIKEMLAANPQDRPdAFELE 326
Cdd:PTZ00283 245 FDGENMEEvmhktLAGRYDPLPPSISPemqeiVTALLSSDPKRR---PSSSKLLNMPICKLFISGLLEIVQTQP-GFSGP 320

                 ....
gi 119628251 327 LRLV 330
Cdd:PTZ00283 321 LRDT 324
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-325 2.21e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 83.71  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI--RCHAPENVELALREFWALSSIksQHPNVIHLEECILQKdgmVQKM 84
Cdd:cd14049    7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKIliKKVTKRDCMKVLREVKVLAGL--QHPNIVGYHTAWMEH---VQLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHgsnssLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNeyllsrkpnrkTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14049   82 LY-----IQMQLCELSLWDWIVERNKRPCEEEFKSAPYTPVDVD-----------VTTKILQQLLEGVTYIHSMGIVHRD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldTSDLEptLKVADFGLSkvCSASGQNPEEPVSVNKCFLST---ACGTDFYMAPEVWEG-HYTAKADI 240
Cdd:cd14049  146 LKPRNIFLH-----GSDIH--VRIGDFGLA--CPDILQDGNDSTTMSRLNGLThtsGVGTCLYAAPEQLEGsHYDFKSDM 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIiwaMLERITFIDTETKKELLGSYVKQGTeiVPvgeallenPKMELLIPVKKKsmngrmkqLIKEMLAANPQDRP 320
Cdd:cd14049  217 YSIGVI---LLELFQPFGTEMERAEVLTQLRNGQ--IP--------KSLCKRWPVQAK--------YIKLLTSTEPSERP 275

                 ....*
gi 119628251 321 DAFEL 325
Cdd:cd14049  276 SASQL 280
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-251 2.55e-18

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 83.91  E-value: 2.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRefwalssiKSQHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKiidKSKRDPSEEIEILMR--------YGQHPNIITLKD------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiAFDprSAYYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14177   66 ---------------------VYD--DGRYVYLVTELMKGGELLDRILRQKFfSEREASAVLYTITKTVDYLHCQGVVHR 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrLDTSDLEPTLKVADFGLSKvcSASGQNPeepvsvnkcFLSTACGTDFYMAPEV-WEGHYTAKADIFA 242
Cdd:cd14177  123 DLKPSNILY----MDDSANADSIRICDFGFAK--QLRGENG---------LLLTPCYTANFVAPEVlMRQGYDAACDIWS 187

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd14177  188 LGVLLYTML 196
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
7-322 2.62e-18

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 83.09  E-value: 2.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCH---APENVELALREFWALSSIksQHPNVI-HLEECIlqkdgmvq 82
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFemmDAKARQDCLKEIDLLQQL--NHPNIIkYLASFI-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNR-----KTNTSFMLQLSSALAFLHK 157
Cdd:cd08224   71 -----ENNELNI-----------------------VLELADAGDLSRLIKHFKKQKrlipeRTIWKYFVQLCSALEHMHS 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSasgqnpEEPVSVNkcflsTACGTDFYMAPEVWEGH-YTA 236
Cdd:cd08224  123 KRIMHRDIKPANVFITAN--------GVVKLGDLGLGRFFS------SKTTAAH-----SLVGTPYYMSPERIREQgYDF 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMleritfidtetkkellgsyvkqgteivpvgeALLENP----KMELLI-----------PVKKKSMN 301
Cdd:cd08224  184 KSDIWSLGCLLYEM-------------------------------AALQSPfygeKMNLYSlckkiekceypPLPADLYS 232
                        330       340
                 ....*....|....*....|.
gi 119628251 302 GRMKQLIKEMLAANPQDRPDA 322
Cdd:cd08224  233 QELRDLVAACIQPDPEKRPDI 253
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
15-325 2.89e-18

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 83.23  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIrchaPENVElalREFWALssiksqhpnviHlEECILQKdgmvqKMSHgSNSSLYL 94
Cdd:cd06624   17 GKGTFGVVYAARDLSTQVRIAIKEI----PERDS---REVQPL-----------H-EEIALHS-----RLSH-KNIVQYL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  95 qlvetslkGEIAFDprsAYYLWFvMDFCDGGDMNEYLLSR----KPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd06624   72 --------GSVSED---GFFKIF-MEQVPGGSLSALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LISQtrldtsdLEPTLKVADFGLSKvcSASGQNPeepvsvnkcFLSTACGTDFYMAPEVWE----GhYTAKADIFALGII 246
Cdd:cd06624  140 LVNT-------YSGVVKISDFGTSK--RLAGINP---------CTETFTGTLQYMAPEVIDkgqrG-YGPPADIWSLGCT 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 247 IWAMLE-RITFIDtetkkelLGSYVkqgTEIVPVGEAllenpKMELLIPvkkKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd06624  201 IIEMATgKPPFIE-------LGEPQ---AAMFKVGMF-----KIHPEIP---ESLSEEAKSFILRCFEPDPDKRATASDL 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
11-251 2.89e-18

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 82.91  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRchapenvelalrefwaLSSI--KSQHPNVIhLEECILqkdgMVQKMSHGS 88
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLK----------------KSDMiaKNQVTNVK-AERAIM----MIQGESPYV 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nSSLYLqlvetslkgeiAFDprSAYYLWFVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05611   60 -AKLYY-----------SFQ--SKDYLYLVMEYLNGGDCASLIktlggLPEDWAKQ----YIAEVVLGVEDLHQRGIIHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQNPEepvsvnkcFLstacGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05611  122 DIKPENLLIDQT--------GHLKLTDFGLSRNGLEKRHNKK--------FV----GTPDYLAPETILGVgDDKMSDWWS 181

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd05611  182 LGCVIFEFL 190
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
7-251 3.11e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 83.71  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENV-ELALREFWALSSIksQHPNVIHLEECILqkdgmvqkm 84
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLeQEDEGVpSTAIREISLLKEM--QHGNIVRLQDVVH--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgSNSSLYL--QLVETSLKGEiafdprsayylwfvMDFCDGGDMNEYLLSrkpnrktntSFMLQLSSALAFLHKNQIIH 162
Cdd:PLN00009  72 ---SEKRLYLvfEYLDLDLKKH--------------MDSSPDFAKNPRLIK---------TYLYQILRGIAYCHSHRVLH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsdlePTLKVADFGLSKvcsASGQnpeePVSVnkcfLSTACGTDFYMAPEVWEG--HYTAKADI 240
Cdd:PLN00009 126 RDLKPQNLLIDRRT-------NALKLADFGLAR---AFGI----PVRT----FTHEVVTLWYRAPEILLGsrHYSTPVDI 187
                        250
                 ....*....|.
gi 119628251 241 FALGIIIWAML 251
Cdd:PLN00009 188 WSVGCIFAEMV 198
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
5-252 3.30e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 83.62  E-value: 3.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSsiKSQHPNVIHLEECILQKDgmvqkm 84
Cdd:cd06654   19 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMR--ENKNPNIVNYLDSYLVGD------ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd06654   91 -----------------------------ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldtsdLEPTLKVADFGLskvCSASgqNPEEPVSvnkcflSTACGTDFYMAPE-VWEGHYTAKADIFAL 243
Cdd:cd06654  142 IKSDNILLG--------MDGSVKLTDFGF---CAQI--TPEQSKR------STMVGTPYWMAPEvVTRKAYGPKVDIWSL 202

                 ....*....
gi 119628251 244 GIIIWAMLE 252
Cdd:cd06654  203 GIMAIEMIE 211
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
5-252 3.42e-18

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: 83.62  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSsiKSQHPNVIHLEECILQKDgmvqkm 84
Cdd:cd06656   18 KKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMR--ENKNPNIVNYLDSYLVGD------ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd06656   90 -----------------------------ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldtsdLEPTLKVADFGLSKVCSasgqnPEEPVSvnkcflSTACGTDFYMAPE-VWEGHYTAKADIFAL 243
Cdd:cd06656  141 IKSDNILLG--------MDGSVKLTDFGFCAQIT-----PEQSKR------STMVGTPYWMAPEvVTRKAYGPKVDIWSL 201

                 ....*....
gi 119628251 244 GIIIWAMLE 252
Cdd:cd06656  202 GIMAIEMVE 210
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
115-332 3.61e-18

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 83.26  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLlsrkpnrKTNTS-------FMLQLSSALAFLH---------KNQIIHRDLKPDNILISqtrld 178
Cdd:cd13998   68 LWLVTAFHPNGSL*DYL-------SLHTIdwvslcrLALSVARGLAHLHseipgctqgKPAIAHRDLKSKNILVK----- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 179 tSDLepTLKVADFGLS-KVCSASGQNPEEPVSvnkcflstACGTDFYMAPEVWEG-----HYTA--KADIFALGIIIWAM 250
Cdd:cd13998  136 -NDG--TCCIADFGLAvRLSPSTGEEDNANNG--------QVGTKRYMAPEVLEGainlrDFESfkRVDIYAMGLVLWEM 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 251 LERITFIDTETKKELLGSYVKQGTEivPVGEALLENPKMELL---IPVKKKSMNG--RMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd13998  205 ASRCTDLFGIVEEYKPPFYSEVPNH--PSFEDMQEVVVRDKQrpnIPNRWLSHPGlqSLAETIEECWDHDAEARLTAQCI 282

                 ....*..
gi 119628251 326 ELRLVQI 332
Cdd:cd13998  283 EERLSEF 289
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
6-252 4.70e-18

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 82.49  E-value: 4.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIR--EVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDgmvqk 83
Cdd:cd06648    5 PRSDLDNfvKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDY--QHPNIVEMYSSYLVGD----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd06648   78 ------------------------------ELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldTSDlePTLKVADFGLskvCsasGQNPEEpVSVNKCFLstacGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd06648  128 DIKSDSILL------TSD--GRVKLSDFGF---C---AQVSKE-VPRRKSLV----GTPYWMAPEVISRLpYGTEVDIWS 188
                        250
                 ....*....|
gi 119628251 243 LGIIIWAMLE 252
Cdd:cd06648  189 LGIMVIEMVD 198
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
14-325 4.83e-18

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 82.45  E-value: 4.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRC-----HAPENVELALREFWALSSIksQHPNvihleecILQKDGMVQKmshGS 88
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLvdddkKSRESVKQLEQEIALLSKL--RHPN-------IVQYYGTERE---ED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVEtslKGEIAfdprsayylwfvmdfcdgGDMNEYLLSRKPNRKTNTSfmlQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd06632   76 NLYIFLEYVP---GGSIH------------------KLLQRYGAFEEPVIRLYTR---QILSGLAYLHSRNTVHRDIKGA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILIsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcFLSTACGTDFYMAPEV---WEGHYTAKADIFALGi 245
Cdd:cd06632  132 NILV--------DTNGVVKLADFGMAKHVEAFS------------FAKSFKGSPYWMAPEVimqKNSGYGLAVDIWSLG- 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 iiwamlerITFIDTETKKELLGSY--VKQGTEIVPVGEallenpkmellIPVKKKSMNGRMKQLIKEMLAANPQDRPDAF 323
Cdd:cd06632  191 --------CTVLEMATGKPPWSQYegVAAIFKIGNSGE-----------LPPIPDHLSPDAKDFIRLCLQRDPEDRPTAS 251

                 ..
gi 119628251 324 EL 325
Cdd:cd06632  252 QL 253
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
14-261 5.05e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 82.27  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGMVqkmshgsnssly 93
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQL--RHPRLLQLYDAFETPREMV------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdprsayylwFVMDFCDGGDMNE------YLLSRKpnrkTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd14103   67 -----------------------LVMEYVAGGELFErvvdddFELTER----DCILFMRQICEGVQYMHKQGILHLDLKP 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsQTRldTSDLeptLKVADFGLskvcsASGQNPEEPVSVNkcflstaCGTDFYMAPEVWegHYTA---KADIFALG 244
Cdd:cd14103  120 ENILC-VSR--TGNQ---IKIIDFGL-----ARKYDPDKKLKVL-------FGTPEFVAPEVV--NYEPisyATDMWSVG 179
                        250       260
                 ....*....|....*....|.
gi 119628251 245 IIIWAMLERIT-FI---DTET 261
Cdd:cd14103  180 VICYVLLSGLSpFMgdnDAET 200
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
5-268 5.37e-18

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 82.18  E-value: 5.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVyEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHleecilqkdgmvqkm 84
Cdd:cd14111    2 QKPYTFLDEKARGRFGVI-RRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALH--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgEIAFDPRsayYLWFVMDFCDGGDMNEYLLSR-KPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14111   66 -------------------EAYITPR---YLVLIAEFCSGKELLHSLIDRfRYSEDDVVGYLVQILQGLEYLHGRRVLHL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRldtsdlepTLKVADFGlskvcSASGQNpeePVSVNKCflSTACGTDFYMAPEVWEGHYTAK-ADIFA 242
Cdd:cd14111  124 DIKPDNIMVTNLN--------AIKIVDFG-----SAQSFN---PLSLRQL--GRRTGTLEYMAPEMVKGEPVGPpADIWS 185
                        250       260       270
                 ....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLE-RITFID---TETKKELLGS 268
Cdd:cd14111  186 IGVLTYIMLSgRSPFEDqdpQETEAKILVA 215
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
7-324 6.71e-18

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 83.29  E-value: 6.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELA---LREFWALSSIKsqHPNVIHLEECILQKdgmvqk 83
Cdd:cd07859    1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDAtriLREIKLLRLLR--HPDIVEIKHIMLPP------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mSHGSNSSLYL--QLVETSLKGEI-AFDPRSAYYLWFvmdfcdggdmneyllsrkpnrktntsFMLQLSSALAFLHKNQI 160
Cdd:cd07859   72 -SRREFKDIYVvfELMESDLHQVIkANDDLTPEHHQF--------------------------FLYQLLRALKYIHTANV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISqtrldtSDLEptLKVADFGLSKVCSASGqnpeePVSVnkcFLSTACGTDFYMAPEV---WEGHYTAK 237
Cdd:cd07859  125 FHRDLKPKNILAN------ADCK--LKICDFGLARVAFNDT-----PTAI---FWTDYVATRWYRAPELcgsFFSKYTPA 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAMLeritfidteTKKELL-GSYVKQGTEIVpvgEALLENPKMELLIPVKKKS-----MNGRMKQ----- 306
Cdd:cd07859  189 IDIWSIGCIFAEVL---------TGKPLFpGKNVVHQLDLI---TDLLGTPSPETISRVRNEKarrylSSMRKKQpvpfs 256
                        330       340       350
                 ....*....|....*....|....*....|
gi 119628251 307 ------------LIKEMLAANPQDRPDAFE 324
Cdd:cd07859  257 qkfpnadplalrLLERLLAFDPKDRPTAEE 286
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
8-255 8.27e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 83.15  E-value: 8.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRefwalssiKSQHPNVIHLEEciLQKDGMvqkm 84
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEEIEILLR--------YGQHPNIITLKD--VYDDGK---- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRK-PNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14176   87 -----------------------------YVYVVTELMKGGELLDKILRQKfFSEREASAVLFTITKTVEYLHAQGVVHR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd14176  138 DLKPSNILY----VDESGNPESIRICDFGFAKQLRAENG-----------LLMTPCYTANFVAPEVLERQgYDAACDIWS 202
                        250
                 ....*....|...
gi 119628251 243 LGIIIWAMLERIT 255
Cdd:cd14176  203 LGVLLYTMLTGYT 215
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
118-325 1.03e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 81.98  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRK--PNRKTNtSFMLQLSSALAFL--HKNQIIHRDLKPDNILisqtrLDTSDLEPTLKVADFGL 193
Cdd:cd13990   83 VLEYCDGNDLDFYLKQHKsiPEREAR-SIIMQVVSALKYLneIKPPIIHYDLKPGNIL-----LHSGNVSGEIKITDFGL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 SKvcsasgQNPEEPVSVNKCFL-STACGTDFYMAPEVWE-----GHYTAKADIFALGIIIWAMLeritfidtetkkellg 267
Cdd:cd13990  157 SK------IMDDESYNSDGMELtSQGAGTYWYLPPECFVvgktpPKISSKVDVWSVGVIFYQML---------------- 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 268 sYVKQgteivPVGEALLENPKMELLIPVK--------KKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd13990  215 -YGRK-----PFGHNQSQEAILEENTILKatevefpsKPVVSSEAKDFIRRCLTYRKEDRPDVLQL 274
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
8-250 1.55e-17

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 81.68  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALREFWALSSIKSqhPNVIHLEECIlqKDgmvqkm 84
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKildKQKVVKLKQVEHTLNEKRILQAINF--PFLVKLEYSF--KD------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLL-SRKPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14209   73 ----NSNLYM-----------------------VMEYVPGGEMFSHLRrIGRFSEPHARFYAAQIVLAFEYLHSLDLIYR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRLdtsdleptLKVADFGLSKVCsasgqnpeepvsvnKCFLSTACGTDFYMAPEVWEGHYTAKA-DIFA 242
Cdd:cd14209  126 DLKPENLLIDQQGY--------IKVTDFGFAKRV--------------KGRTWTLCGTPEYLAPEIILSKGYNKAvDWWA 183

                 ....*...
gi 119628251 243 LGIIIWAM 250
Cdd:cd14209  184 LGVLIYEM 191
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7-251 1.73e-17

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 80.97  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCHA-PENVElalREFWALSSIKsqHPNVIHLEECILqkdgmvqkm 84
Cdd:cd14662    1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIeRGLKiDENVQ---REIINHRSLR--HPNIIRFKEVVL--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd14662   67 --------------------------TPTHLAIVMEYAAGGELFERICNAGRFSEDEARYFFqQLISGVSYCHSMQICHR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILisqtrLDTSDlEPTLKVADFGLSKvCSASGQNPEEPVsvnkcflstacGTDFYMAPEVW-EGHYTAK-ADIF 241
Cdd:cd14662  121 DLKLENTL-----LDGSP-APRLKICDFGYSK-SSVLHSQPKSTV-----------GTPAYIAPEVLsRKEYDGKvADVW 182
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14662  183 SCGVTLYVML 192
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
7-253 1.87e-17

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 81.42  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN--VELALREFwALSSIKSQHPNVIHLeecilqkdgmvqkm 84
Cdd:cd07837    2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEgvPSTALREV-SLLQMLSQSIYIVRL-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnssLYLQLVETslkgeiafDPRSAYYLwfVMDFCDgGDMNEYLLS--RKPNR----KTNTSFMLQLSSALAFLHKN 158
Cdd:cd07837   67 -------LDVEHVEE--------NGKPLLYL--VFEYLD-TDLKKFIDSygRGPHNplpaKTIQSFMYQLCKGVAHCHSH 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQTRLdtsdlepTLKVADFGLSKVCSAsgqnpeePVsvnKCFLSTACgTDFYMAPEVWEG--HYTA 236
Cdd:cd07837  129 GVMHRDLKPQNLLVDKQKG-------LLKIADLGLGRAFTI-------PI---KSYTHEIV-TLWYRAPEVLLGstHYST 190
                        250
                 ....*....|....*..
gi 119628251 237 KADIFALGIIIWAMLER 253
Cdd:cd07837  191 PVDMWSVGCIFAEMSRK 207
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
7-251 2.35e-17

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 81.92  E-value: 2.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrcHAPENVEL-ALREFWALSSIKS-QHPNVIHLEECilqkdgmvqkm 84
Cdd:cd07880   16 RYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKL--YRPFQSELfAKRAYRELRLLKHmKHENVIGLLDV----------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetsLKGEIAFDPRSAYYLwfVMDFCdGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd07880   83 ----------------FTPDLSLDRFHDFYL--VMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQtrldtsdlEPTLKVADFGLSKvcsasgQNPEEpvsvnkcfLSTACGTDFYMAPEV---WEgHYTAKADIF 241
Cdd:cd07880  144 LKPGNLAVNE--------DCELKILDFGLAR------QTDSE--------MTGYVVTRWYRAPEVilnWM-HYTQTVDIW 200
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd07880  201 SVGCIMAEML 210
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
8-322 2.37e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 80.84  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRefwalssiKSQHPNVIHLEEciLQKDGMvqkm 84
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKvidKSKRDPSEEIEILLR--------YGQHPNIITLKD--VYDDGK---- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHR 163
Cdd:cd14175   69 -----------------------------HVYLVTELMRGGELLDKILRQKFFSEREASSVLHtICKTVEYLHSQGVVHR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSAsgqnpeepvsvNKCFLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd14175  120 DLKPSNILY----VDESGNPESLRICDFGFAKQLRA-----------ENGLLMTPCYTANFVAPEVLKRQgYDEGCDIWS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLERIT-FID--TETKKELL-----GSYVKQGTEIVPVGEAllenpkmellipvkkksmngrMKQLIKEMLAA 314
Cdd:cd14175  185 LGILLYTMLAGYTpFANgpSDTPEEILtrigsGKFTLSGGNWNTVSDA---------------------AKDLVSKMLHV 243

                 ....*...
gi 119628251 315 NPQDRPDA 322
Cdd:cd14175  244 DPHQRLTA 251
pknD PRK13184
serine/threonine-protein kinase PknD;
7-319 3.29e-17

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 82.90  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENvELALREFWALSSIKSQ--HPNVIHLEECILQKDGMVQKM 84
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSEN-PLLKKRFLREAKIAADliHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYlQLVETSLKGEIAFDPrsayylwfvmdfcdggdmneylLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:PRK13184  82 PYIEGYTLK-SLLKSVWQKESLSKE----------------------LAEKTSVGAFLSIFHKICATIEYVHSKGVLHRD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldtsdLEPTLKVADFGLSKVCSASgQNPEEPVSVNK---CFLSTA-----CGTDFYMAPEVWEGH-YT 235
Cdd:PRK13184 139 LKPDNILLG--------LFGEVVILDWGAAIFKKLE-EEDLLDIDVDErniCYSSMTipgkiVGTPDYMAPERLLGVpAS 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAMLE-RITFIDTETKKELLGSYVKQGTEIVPVGEallenpkmellIPvkkksmnGRMKQLIKEMLAA 314
Cdd:PRK13184 210 ESTDIYALGVILYQMLTlSFPYRRKKGRKISYRDVILSPIEVAPYRE-----------IP-------PFLSQIAMKALAV 271

                 ....*
gi 119628251 315 NPQDR 319
Cdd:PRK13184 272 DPAER 276
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7-325 3.52e-17

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 80.54  E-value: 3.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHAPENVElalREFWALSSIKsqHPNVIHLEECIlQKDGMv 81
Cdd:cd14086    2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKiintkKLSARDHQKLE---REARICRLLK--HPNIVRLHDSI-SEEGF- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsaYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQI 160
Cdd:cd14086   75 -------------------------------HYL--VFDLVTGGELFEDIVAREFYSEADASHcIQQILESVNHCHQNGI 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILisqtrLDTSDLEPTLKVADFGLSkvCSASGQNPEepvsvnkcFLSTAcGTDFYMAPEVW-EGHYTAKAD 239
Cdd:cd14086  122 VHRDLKPENLL-----LASKSKGAAVKLADFGLA--IEVQGDQQA--------WFGFA-GTPGYLSPEVLrKDPYGKPVD 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERI-TFIDTETKKelLGSYVKQGTEIVPvgealleNPKMELLIPvkkksmngRMKQLIKEMLAANPQD 318
Cdd:cd14086  186 IWACGVILYILLVGYpPFWDEDQHR--LYAQIKAGAYDYP-------SPEWDTVTP--------EAKDLINQMLTVNPAK 248

                 ....*..
gi 119628251 319 RPDAFEL 325
Cdd:cd14086  249 RITAAEA 255
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
115-321 4.39e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 79.67  E-value: 4.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGL 193
Cdd:cd14188   76 IYILLEYCSRRSMAHILKARKVLTEPEVRYYLrQIVSGLKYLHEQEILHRDLKLGNFFINENM--------ELKVGDFGL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 SKVCSASGQNPEepvsvnkcflsTACGTDFYMAPEVW--EGHyTAKADIFALGIIIWAMLERITFIDTETKKELLGSyvk 271
Cdd:cd14188  148 AARLEPLEHRRR-----------TICGTPNYLSPEVLnkQGH-GCESDIWALGCVMYTMLLGRPPFETTNLKETYRC--- 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119628251 272 qgteivpVGEALLENPkmellipvkkKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd14188  213 -------IREARYSLP----------SSLLAPAKHLIASMLSKNPEDRPS 245
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
8-251 4.46e-17

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 79.86  E-value: 4.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREfwalssiksqhpnvihleeciLQKDGMVQKMSHG 87
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKN---------------------LRREGRIQQMIRH 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQLVETSlkgeiafdprSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd14070   63 PNITQLLDILETE----------NSYYL--VMELCPGGNLMHRIYDKKRLEEREARrYIRQLVSAVEHLHRAGVVHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILisqtrLDTSDlepTLKVADFGLSKVCSASGQNPEepvsvnkcfLSTACGTDFYMAPEVWeGH--YTAKADIFALG 244
Cdd:cd14070  131 IENLL-----LDEND---NIKLIDFGLSNCAGILGYSDP---------FSTQCGSPAYAAPELL-ARkkYGPKVDVWSIG 192

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd14070  193 VNMYAML 199
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
118-325 5.65e-17

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 79.33  E-value: 5.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEyLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTsdlepTLKVADFGLSK 195
Cdd:cd14012   82 LTEYAPGGSLSE-LLDSVGSVPLDTarRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTG-----IVKLTDYSLGK 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 196 vcsasgqnpeEPVSVNKCFLSTACGTDFYMAPEVWEGH--YTAKADIFALGIIIWAMLEritfidtetkkellGSYVKQg 273
Cdd:cd14012  156 ----------TLLDMCSRGSLDEFKQTYWLPPELAQGSksPTRKTDVWDLGLLFLQMLF--------------GLDVLE- 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119628251 274 teivpvgeallenpKMELLIPVK-KKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14012  211 --------------KYTSPNPVLvSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
15-251 7.83e-17

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 79.20  E-value: 7.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAviRKTSARVAVKKIRCHAPEN-----VELALREFWALSSIKSQhpnvihleeCILQKDGMVqkMSHGSN 89
Cdd:cd14000    3 GDGGFGSVYRA--SYKGEPVAVKIFNKHTSSNfanvpADTMLRHLRATDAMKNF---------RLLRQELTV--LSHLHH 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 SSLyLQLVETSLKgeiafdPRSayylwFVMDFCDGGDMN----EYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14000   70 PSI-VYLLGIGIH------PLM-----LVLELAPLGSLDhllqQDSRSFASlGRTLQQRIALQVADGLRYLHSAMIIYRD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQtrLDTSDLePTLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDFYMAPEVWEGH--YTAKADIFA 242
Cdd:cd14000  138 LKSHNVLVWT--LYPNSA-IIIKIADYGISRQCCRMGAKGSE-------------GTPGFRAPEIARGNviYNEKVDVFS 201

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd14000  202 FGMLLYEIL 210
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
14-251 8.09e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 79.32  E-value: 8.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIrkTSARVAVKKIRcHAP--------ENVELALREFWALSsiksqHPNVIHLEECILQkdgmvqkms 85
Cdd:cd14145   14 IGIGGFGKVYRAIW--IGDEVAVKAAR-HDPdedisqtiENVRQEAKLFAMLK-----HPNIIALRGVCLK--------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafDPRsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQI---IH 162
Cdd:cd14145   77 ----------------------EPN----LCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtRLDTSDL-EPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTACGTDFYMAPEVWEGHYTAK-ADI 240
Cdd:cd14145  131 RDLKSSNILILE-KVENGDLsNKILKITDFGLAR-------------EWHRTTKMSAAGTYAWMAPEVIRSSMFSKgSDV 196
                        250
                 ....*....|.
gi 119628251 241 FALGIIIWAML 251
Cdd:cd14145  197 WSYGVLLWELL 207
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
5-252 9.63e-17

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 79.38  E-value: 9.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSqhPNVIHLEECILQKDgmvqkm 84
Cdd:cd06655   18 KKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKN--PNIVNFLDSFLVGD------ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd06655   90 -----------------------------ELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldtsdLEPTLKVADFGLSKVCSasgqnPEEPVSvnkcflSTACGTDFYMAPE-VWEGHYTAKADIFAL 243
Cdd:cd06655  141 IKSDNVLLG--------MDGSVKLTDFGFCAQIT-----PEQSKR------STMVGTPYWMAPEvVTRKAYGPKVDIWSL 201

                 ....*....
gi 119628251 244 GIIIWAMLE 252
Cdd:cd06655  202 GIMAIEMVE 210
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
8-251 1.09e-16

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 78.92  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREV-GRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFwalssiksqhpnvihleECILQKDGmvqkmsh 86
Cdd:cd14174    3 YRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREV-----------------ETLYQCQG------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsNSSLyLQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd14174   59 --NKNI-LELIEF-------FEDDTRFYL--VFEKLRGGSILAHIQKRKHfNEREASRVVRDIASALDFLHTKGIAHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILIsqtrlDTSDLEPTLKVADFGLS---KVCSASgqnpeEPVSVNKcfLSTACGTDFYMAPEVWE------GHYTA 236
Cdd:cd14174  127 KPENILC-----ESPDKVSPVKICDFDLGsgvKLNSAC-----TPITTPE--LTTPCGSAEYMAPEVVEvftdeaTFYDK 194
                        250
                 ....*....|....*
gi 119628251 237 KADIFALGIIIWAML 251
Cdd:cd14174  195 RCDLWSLGVILYIML 209
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
8-319 1.11e-16

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 80.08  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTS---ARVAVKKIRCHAPENVELALREFWALSSiKSQHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd05618   22 FDLLRVIGRGSYAKVLLVRLKKTEriyAMKVVKKELVNDDEDIDWVQTEKHVFEQ-ASNHPFLVGLHSCF---------- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdpRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd05618   91 -------------------------QTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSaEISLALNYLHERGIIYR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsaSGQNPEEPVsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05618  146 DLKLDNVLL--------DSEGHIKLTDYGMCK----EGLRPGDTT-------STFCGTPNYIAPEILRGEdYGFSVDWWA 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 243 LGIIIWAMLERITFIDtetkkeLLGSY--VKQGTEIVpVGEALLENpkmELLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd05618  207 LGVLMFEMMAGRSPFD------IVGSSdnPDQNTEDY-LFQVILEK---QIRIP---RSLSVKAASVLKSFLNKDPKER 272
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
8-251 1.11e-16

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 78.68  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVV-----YEAVIRKTSARVAVKKIR---CHAPENVELALREFWALSSIKsqHPNVIHLEEcilqkdg 79
Cdd:cd14076    3 YILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRrdtQQENCQTSKIMREINILKGLT--HPNIVRLLD------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 mvqkmshgsnsslylqLVETSlkgeiafdprsaYYLWFVMDFCDGGDMNEYLLS-RKPNRKTNTSFMLQLSSALAFLHKN 158
Cdd:cd14076   74 ----------------VLKTK------------KYIGIVLEFVSGGELFDYILArRRLKDSVACRLFAQLISGVAYLHKK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASgqNPEepvsvnkcFLSTACGTDFYMAPE--VWEGHYTA 236
Cdd:cd14076  126 GVVHRDLKLENLLLDKNR--------NLVITDFGFANTFDHF--NGD--------LMSTSCGSPCYAAPElvVSDSMYAG 187
                        250
                 ....*....|....*.
gi 119628251 237 -KADIFALGIIIWAML 251
Cdd:cd14076  188 rKADIWSCGVILYAML 203
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
15-329 1.12e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 78.46  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSarVAVKKIRCHApeNVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkmshgsnsslyl 94
Cdd:cd14068    3 GDGGFGSVYRAVYRGED--VAVKIFNKHT--SFRLLRQELVVLSHLH--HPSLVAL------------------------ 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  95 qlvetsLKGEIAfdPRSayylwFVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14068   53 ------LAAGTA--PRM-----LVMELAPKGSLDALLQQDNAslTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SQTRldtSDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcfLSTACGTDFYMAPEVWEGH--YTAKADIFALGIIIWAM 250
Cdd:cd14068  120 FTLY---PNCAIIAKIADYGIAQYCCRMG-------------IKTSEGTPGFRAPEVARGNviYNQQADVYSFGLLLYDI 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 251 L---ERIT--------FIDTETKKELLGSYVKQGTEIVPVGEALlenpkmellipvkkksmngrMKQLIKEmlaaNPQDR 319
Cdd:cd14068  184 LtcgERIVeglkfpneFDELAIQGKLPDPVKEYGCAPWPGVEAL--------------------IKDCLKE----NPQCR 239
                        330
                 ....*....|
gi 119628251 320 PDAFELELRL 329
Cdd:cd14068  240 PTSAQVFDIL 249
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
14-320 1.15e-16

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 78.36  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIrchapenvelalrefwalssiksqhpnvihlEECILQKDGMVQKMSHgsNSSLY 93
Cdd:cd14186    9 LGKGSFACVYRARSLHTGLEVAIKMI-------------------------------DKKAMQKAGMVQRVRN--EVEIH 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVETSLKgEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSR-KPNRKTNT-SFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd14186   56 CQLKHPSIL-ELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRkKPFTEDEArHFMHQIVTGMLYLHSHGILHRDLTLSNLL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 ISQtrldtsdlEPTLKVADFGLskvcSASGQNPEEpvsvnKCFlsTACGTDFYMAPEV-WEGHYTAKADIFALGIIIWAM 250
Cdd:cd14186  135 LTR--------NMNIKIADFGL----ATQLKMPHE-----KHF--TMCGTPNYISPEIaTRSAHGLESDVWSLGCMFYTL 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 251 LERITFIDTETKKELLGSYVkqgteivpvgealLENPKMELLIPVKKKSmngrmkqLIKEMLAANPQDRP 320
Cdd:cd14186  196 LVGRPPFDTDTVKNTLNKVV-------------LADYEMPAFLSREAQD-------LIHQLLRKNPADRL 245
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
14-254 1.28e-16

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 78.30  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEaVIRKTSARVAVKKIRCHAPENVELaLREFWALSsiKSQHPNVI-HLEECILQKDgmvqkmshgsnssl 92
Cdd:cd14065    1 LGKGFFGEVYK-VTHRETGKVMVMKELKRFDEQRSF-LKEVKLMR--RLSHPNILrFIGVCVKDNK-------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd14065   63 ----------------------LNFITEYVNGGTLEELLKSMDEqlPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNC 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LISQtrldtSDLEPTLKVADFGLS-KVCSASGQNPEEPVSVNkcflstACGTDFYMAPEVWEGH-YTAKADIFALGIIIW 248
Cdd:cd14065  121 LVRE-----ANRGRNAVVADFGLArEMPDEKTKKPDRKKRLT------VVGSPYWMAPEMLRGEsYDEKVDVFSFGIVLC 189

                 ....*.
gi 119628251 249 AMLERI 254
Cdd:cd14065  190 EIIGRV 195
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
16-261 1.55e-16

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 78.52  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  16 RGSYGVVYEAviRKTSARVAVKKIRcHAPENVELALREFWALSSIKsqHPNVIHLeecilqkdgmvqkmsHGSNSslylq 95
Cdd:cd14053    5 RGRFGAVWKA--QYLNRLVAVKIFP-LQEKQSWLTEREIYSLPGMK--HENILQF---------------IGAEK----- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  96 lVETSLKGEiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH----------KNQIIHRDL 165
Cdd:cd14053   60 -HGESLEAE----------YWLITEFHERGSLCDYLKGNVISWNELCKIAESMARGLAYLHedipatngghKPSIAHRDF 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISqtrldtSDLepTLKVADFGLSKVCSAsGQNPEEpvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKA----D 239
Cdd:cd14053  129 KSKNVLLK------SDL--TACIADFGLALKFEP-GKSCGD--------THGQVGTRRYMAPEVLEGaiNFTRDAflriD 191
                        250       260
                 ....*....|....*....|..
gi 119628251 240 IFALGIIIWAMLERITFIDTET 261
Cdd:cd14053  192 MYAMGLVLWELLSRCSVHDGPV 213
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
7-247 1.63e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 78.69  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC-HAPENVEL-ALREFWALSSIksQHPNVIHLEECILQK-DGMVQK 83
Cdd:cd07864    8 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPItAIREIKILRQL--NHRSVVNLKEIVTDKqDALDFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGsnsslylqlvetslkgeiafdprsAYYLWF-VMDFCDGGDMNEYLLSRkpNRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd07864   86 KDKG------------------------AFYLVFeYMDHDLMGLLESGLVHF--SEDHIKSFMKQLLEGLNYCHKKNFLH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPeepvSVNKCFlstacgTDFYMAPEVWEGH--YTAKADI 240
Cdd:cd07864  140 RDIKCSNILLNN--------KGQIKLADFGLARLYNSEESRP----YTNKVI------TLWYRPPELLLGEerYGPAIDV 201

                 ....*..
gi 119628251 241 FALGIII 247
Cdd:cd07864  202 WSCGCIL 208
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
115-251 1.63e-16

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 78.86  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05603   71 LYFVLDYVNGGELFFHLQRERCFLEPRARFyAAEVASAIGYLHSLNIIYRDLKPENILL--------DCQGHVVLTDFGL 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 194 SKvcsaSGQNPEEPVsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05603  143 CK----EGMEPEETT-------STFCGTPEYLAPEVLRKEpYDRTVDWWCLGAVLYEML 190
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
8-251 1.67e-16

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 78.53  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREV-GRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSqHPNVihleecilqkdgmvqkmsh 86
Cdd:cd14173    3 YQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQG-HRNV------------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslyLQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHRDL 165
Cdd:cd14173   63 -------LELIEF-------FEEEDKFYL--VFEKMRGGSILSHIHRRRHFNELEASVVVQdIASALDFLHNKGIAHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILIsqtrlDTSDLEPTLKVADFGLSKVCSASGQNpeEPVSVNKcfLSTACGTDFYMAPEVWEGH------YTAKAD 239
Cdd:cd14173  127 KPENILC-----EHPNQVSPVKICDFDLGSGIKLNSDC--SPISTPE--LLTPCGSAEYMAPEVVEAFneeasiYDKRCD 197
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd14173  198 LWSLGVILYIML 209
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
11-253 1.90e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 78.53  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL---ALREFWALSSIKsqHPNVIHLEECILQKdgmvqkmshg 87
Cdd:cd06634   20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwqdIIKEVKFLQKLR--HPNTIEYRGCYLRE---------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLS-SALAFLHKNQIIHRDLK 166
Cdd:cd06634   88 -------------------------HTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGAlQGLAYLHSHNMIHRDVK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRLdtsdleptLKVADFGlskvcSASGQNPEepvsvnkcflSTACGTDFYMAPEVW----EGHYTAKADIFA 242
Cdd:cd06634  143 AGNILLTEPGL--------VKLGDFG-----SASIMAPA----------NSFVGTPYWMAPEVIlamdEGQYDGKVDVWS 199
                        250
                 ....*....|.
gi 119628251 243 LGIIIWAMLER 253
Cdd:cd06634  200 LGITCIELAER 210
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
8-245 2.08e-16

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 78.13  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR-CH-APENVELALREFWALSSiksqHPNVIHLEecilqkdGMVQKMs 85
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpIHdIDEEIEAEYNILKALSD----HPNVVKFY-------GMYYKK- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiafDPRSAYYLWFVMDFCDGGDMNEYL--LSRKPNRKTNTSFMLQLSSAL---AFLHKNQI 160
Cdd:cd06638   88 ----------------------DVKNGDQLWLVLELCNGGSVTDLVkgFLKRGERMEEPIIAYILHEALmglQHLHVNKT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnKCFLSTACGTDFYMAPEV------WEGHY 234
Cdd:cd06638  146 IHRDVKGNNILLTT--------EGGVKLVDFGVSAQLTST-----------RLRRNTSVGTPFWMAPEViaceqqLDSTY 206
                        250
                 ....*....|.
gi 119628251 235 TAKADIFALGI 245
Cdd:cd06638  207 DARCDVWSLGI 217
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
115-254 2.08e-16

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 78.08  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLsrkpNRKTNTSFMLQL----SSALAFLH--------KNQIIHRDLKPDNILISqtrldtSDL 182
Cdd:cd14056   68 LWLITEYHEHGSLYDYLQ----RNTLDTEEALRLaysaASGLAHLHteivgtqgKPAIAHRDLKSKNILVK------RDG 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 183 epTLKVADFGLSkVCSASGQNPeEPVSVNKcflstACGTDFYMAPEVWEG--------HYTaKADIFALGIIIWAMLERI 254
Cdd:cd14056  138 --TCCIADLGLA-VRYDSDTNT-IDIPPNP-----RVGTKRYMAPEVLDDsinpksfeSFK-MADIYSFGLVLWEIARRC 207
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
8-251 2.12e-16

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 77.62  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGMVqkmshg 87
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQL--HHPKLINLHDAFEDDNEMV------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSR--KPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd14114   76 -----------------------------LILEFLSGGELFERIAAEhyKMSEAEVINYMRQVCEGLCHMHENNIVHLDI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILIsQTRLDTSdleptLKVADFGLskvcsASGQNPEEPVSVNKcflstacGTDFYMAPEVWE----GHYTakaDIF 241
Cdd:cd14114  127 KPENIMC-TTKRSNE-----VKLIDFGL-----ATHLDPKESVKVTT-------GTAEFAAPEIVErepvGFYT---DMW 185
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14114  186 AVGVLSYVLL 195
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
114-251 2.18e-16

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 78.45  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEYLLSR-KPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFG 192
Cdd:cd05620   70 HLFFVMEFLNGGDLMFHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML--------DRDGHIKIADFG 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 193 LSKvcsasgqnpEEPVSVNKCflSTACGTDFYMAPEVWEG-HYTAKADIFALGIIIWAML 251
Cdd:cd05620  142 MCK---------ENVFGDNRA--STFCGTPDYIAPEILQGlKYTFSVDWWSFGVLLYEML 190
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
14-319 2.51e-16

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 78.08  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCH-APENvelalREFWALS---SIKSQHPNVIHLEECilqKDGMvQKMSHGSn 89
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQElSPKN-----RERWCLEiqiMKRLNHPNVVAARDV---PEGL-QKLAPND- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sslyLQLVetslkgeiafdprsayylwfVMDFCDGGDMNEYLlsrkpNRKTNT---------SFMLQLSSALAFLHKNQI 160
Cdd:cd14038   72 ----LPLL--------------------AMEYCQGGDLRKYL-----NQFENCcglregailTLLSDISSALRYLHENRI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQ--TRLdtsdlepTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTA-CGTDFYMAPEVWEGH-YTA 236
Cdd:cd14038  123 IHRDLKPENIVLQQgeQRL-------IHKIIDLGYAK-------------ELDQGSLCTSfVGTLQYLAPELLEQQkYTV 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWamlERIT----FIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVK---KKSMNGRMKQLIK 309
Cdd:cd14038  183 TVDYWSFGTLAF---ECITgfrpFLPNWQPVQWHGKVRQKSNEDIVVYEDLTGAVKFSSVLPTPnnlNGILAGKLERWLQ 259
                        330
                 ....*....|
gi 119628251 310 EMLAANPQDR 319
Cdd:cd14038  260 CMLMWHPRQR 269
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
14-251 2.68e-16

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 77.57  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPeNVELALREFWALSSIKSQhpnVIHLEEciLQKDGMVQKMshGSNSSly 93
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELPSV-SAENKDRKKSMLDALQRE---IALLRE--LQHENIVQYL--GSSSD-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdprsAYYLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd06628   78 ------------------ANHLNIFLEYVPGGSVATLLNNYGAfEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 sqtrldtsDLEPTLKVADFGLSK---VCSASGQNPEEPVSVNkcflstacGTDFYMAPEVW-EGHYTAKADIFALGIIIW 248
Cdd:cd06628  140 --------DNKGGIKISDFGISKkleANSLSTKNNGARPSLQ--------GSVFWMAPEVVkQTSYTRKADIWSLGCLVV 203

                 ...
gi 119628251 249 AML 251
Cdd:cd06628  204 EML 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
8-265 2.93e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 77.74  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVE-LALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkmsH 86
Cdd:cd07871    7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPcTAIREVSLLKNLK--HANIVTLHDII-----------H 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNS-SLYLQLVETSLKgeiafdprsaYYLwfvmDFCdGGDMNEYllsrkpNRKTntsFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07871   74 TERClTLVFEYLDSDLK----------QYL----DNC-GNLMSMH------NVKI---FMFQLLRGLSYCHKRKILHRDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFAL 243
Cdd:cd07871  130 KPQNLLINE--------KGELKLADFGLARAKSVPTKT-----------YSNEVVTLWYRPPDVLLGstEYSTPIDMWGV 190
                        250       260
                 ....*....|....*....|...
gi 119628251 244 GIIIWAMLE-RITFIDTETKKEL 265
Cdd:cd07871  191 GCILYEMATgRPMFPGSTVKEEL 213
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
5-325 3.29e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 77.38  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIhleecilqkdgmvqkM 84
Cdd:cd06646    8 QHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECK--HCNIV---------------A 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSnsslYLqlvetslkgeiafdprSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLS-SALAFLHKNQIIHR 163
Cdd:cd06646   71 YFGS----YL----------------SREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETlQGLAYLHSKGKMHR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrlDTSDleptLKVADFGLSKVCSASgqnpeepVSVNKCFLstacGTDFYMAPEVW----EGHYTAKAD 239
Cdd:cd06646  131 DIKGANILLT----DNGD----VKLADFGVAAKITAT-------IAKRKSFI----GTPYWMAPEVAavekNGGYNQLCD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLE-RITFIDTETKKELLgsyvkqgteivPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQD 318
Cdd:cd06646  192 IWAVGITAIELAElQPPMFDLHPMRALF-----------LMSKSNFQPPKLK-----DKTKWSSTFHNFVKISLTKNPKK 255

                 ....*..
gi 119628251 319 RPDAFEL 325
Cdd:cd06646  256 RPTAERL 262
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
10-251 3.57e-16

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 78.04  E-value: 3.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSsIKSQHPNVIHLEeCILQkdgmvqkmsh 86
Cdd:cd05619    9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVvlmDDDVECTMVEKRVLS-LAWEHPFLTHLF-CTFQ---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprSAYYLWFVMDFCDGGDMNEYLLS-RKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05619   77 ------------------------TKENLFFVMEYLNGGDLMFHIQScHKFDLPRATFYAAEIICGLQFLHSKGIVYRDL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpEEPVSVNKCflSTACGTDFYMAPEVWEGH-YTAKADIFALG 244
Cdd:cd05619  133 KLDNILL--------DKDGHIKIADFGMCK---------ENMLGDAKT--STFCGTPDYIAPEILLGQkYNTSVDWWSFG 193

                 ....*..
gi 119628251 245 IIIWAML 251
Cdd:cd05619  194 VLLYEML 200
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
6-324 5.13e-16

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 77.20  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHAPENVELALREFWALSSIKsqHPNVIHLEECIlqkdgm 80
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKivdvaKFTSSPGLSTEDLKREASICHMLK--HPHIVELLETY------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  81 vqkmshgsnsslylqlvetslkgeiafdpRSAYYLWFVMDFCDGGDMNEYLLSRKPN-----RKTNTSFMLQLSSALAFL 155
Cdd:cd14094   75 -----------------------------SSDGMLYMVFEFMDGADLCFEIVKRADAgfvysEAVASHYMRQILEALRYC 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILisqtrLDTSDLEPTLKVADFGLSKVCSASGqnpeepvsvnkcflSTAC---GTDFYMAPEVWEG 232
Cdd:cd14094  126 HDNNIIHRDVKPHCVL-----LASKENSAPVKLGGFGVAIQLGESG--------------LVAGgrvGTPHFMAPEVVKR 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 H-YTAKADIFALGIIIWAMLE-RITFIDTetkKELLGSYVKQGTeiVPVgealleNPKMEllipvkkKSMNGRMKQLIKE 310
Cdd:cd14094  187 EpYGKPVDVWGCGVILFILLSgCLPFYGT---KERLFEGIIKGK--YKM------NPRQW-------SHISESAKDLVRR 248
                        330
                 ....*....|....
gi 119628251 311 MLAANPQDRPDAFE 324
Cdd:cd14094  249 MLMLDPAERITVYE 262
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
7-319 5.92e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 76.96  E-value: 5.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVEL---ALREFWALSSIKSQhpNVIHLEEcilqkdgmvqk 83
Cdd:cd07848    2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFK-DSEENEEVketTLRELKMLRTLKQE--NIVELKE----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGgDMNEyLLSRKPN---RKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd07848   68 ----------------------AFRRRGKLYL--VFEYVEK-NMLE-LLEEMPNgvpPEKVRSYIYQLIKAIHWCHKNDI 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCS-ASGQNPEEPVSvnkcflstacgTDFYMAPEVWEGHYTAKA- 238
Cdd:cd07848  122 VHRDIKPENLLISHNDV--------LKLCDFGFARNLSeGSNANYTEYVA-----------TRWYRSPELLLGAPYGKAv 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALL-ENPKME-LLIPVKKKS----------MNGRMKQ 306
Cdd:cd07848  183 DMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFySNPRFHgLRFPAVNHPqslerrylgiLSGVLLD 262
                        330
                 ....*....|...
gi 119628251 307 LIKEMLAANPQDR 319
Cdd:cd07848  263 LMKNLLKLNPTDR 275
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
8-325 6.38e-16

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 76.57  E-value: 6.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYeaVIRKTSAR--VAVKKIRCHAPENVELALREfwALSSIKSQHPNVIHLEECILQKDGmvqkms 85
Cdd:cd13986    2 YRIQRLLGEGGFSFVY--LVEDLSTGrlYALKKILCHSKEDVKEAMRE--IENYRLFNHPNILRLLDSQIVKEA------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hGSNSSLYLQLvetslkgeiafdprsAYY----LWFVMDFCDggDMNEYLlsrkPNRKTnTSFMLQLSSALAFLHKNQII 161
Cdd:cd13986   72 -GGKKEVYLLL---------------PYYkrgsLQDEIERRL--VKGTFF----PEDRI-LHIFLGICRGLKAMHEPELV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 ---HRDLKPDNILISqtrldtSDLEPTLkvADFGLSKVCSASGQNPEEPVSVnKCFLSTACgTDFYMAPEVW--EGHYT- 235
Cdd:cd13986  129 pyaHRDIKPGNVLLS------EDDEPIL--MDLGSMNPARIEIEGRREALAL-QDWAAEHC-TMPYRAPELFdvKSHCTi 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 -AKADIFALGIIIWAMLERITFIDTEtkkellgsyVKQGTeivPVGEALLENpkmeLLIPVKKKSMNGRMKQLIKEMLAA 314
Cdd:cd13986  199 dEKTDIWSLGCTLYALMYGESPFERI---------FQKGD---SLALAVLSG----NYSFPDNSRYSEELHQLVKSMLVV 262
                        330
                 ....*....|.
gi 119628251 315 NPQDRPDAFEL 325
Cdd:cd13986  263 NPAERPSIDDL 273
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
114-251 6.98e-16

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 77.27  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEyLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADF 191
Cdd:cd05599   75 NLYLIMEFLPGGDMMT-LLMKKDTLTEEETrfYIAETVLAIESIHKLGYIHRDIKPDNLLL--------DARGHIKLSDF 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 192 GLSKvcsasgqnpeePVSVNKCFLSTAcGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05599  146 GLCT-----------GLKKSHLAYSTV-GTPDYIAPEVFLQKgYGKECDWWSLGVIMYEML 194
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
7-252 7.11e-16

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 77.23  E-value: 7.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVeLALREFWALSSIKS-QHPNVIHLeecilqkdgmvqkms 85
Cdd:cd07856   11 RYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPV-LAKRTYRELKLLKHlRHENIISL--------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnSSLYLQLVETslkgeiafdprsayyLWFVMDFCdGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07856   75 ----SDIFISPLED---------------IYFVTELL-GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTrldtsdlePTLKVADFGLSKVcsasgQNPEepvsvnkcfLSTACGTDFYMAPEV---WEgHYTAKADIFA 242
Cdd:cd07856  135 KPSNILVNEN--------CDLKICDFGLARI-----QDPQ---------MTGYVSTRYYRAPEImltWQ-KYDVEVDIWS 191
                        250
                 ....*....|
gi 119628251 243 LGIIIWAMLE 252
Cdd:cd07856  192 AGCIFAEMLE 201
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
14-251 7.19e-16

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 76.21  E-value: 7.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRchaPENVELA--LREFwALSSIKSQHPNVIhleecilqkdgmvqkmshgsnsS 91
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVP---KPSTKLKdfLREY-NISLELSVHPHII----------------------K 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 LYlqlvetslkgEIAFDPRSAYYlwFVMDFCDGGDMNEYLLSR----KPNRKtntSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd13987   55 TY----------DVAFETEDYYV--FAQEYAPYGDLFSIIPPQvglpEERVK---RCAAQLASALDFMHSKNLVHRDIKP 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISqtrldTSDLEpTLKVADFGL-----SKVCSASGQNPeepvsvnkcflstacgtdfYMAPEVWEghyTAKA---- 238
Cdd:cd13987  120 ENVLLF-----DKDCR-RVKLCDFGLtrrvgSTVKRVSGTIP-------------------YTAPEVCE---AKKNegfv 171
                        250
                 ....*....|....*...
gi 119628251 239 -----DIFALGIIIWAML 251
Cdd:cd13987  172 vdpsiDVWAFGVLLFCCL 189
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
8-247 8.43e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 76.81  E-value: 8.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRC----HAPENVELALrefwaLSSIKSQHPNvihleecilQKDGMVQK 83
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNkkrfHQQALVEVKI-----LKHLNDNDPD---------DKHNIVRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHgsnsslylqlvetslkgeiaFDPRSayYLWFVMDFCDggdMNEYLLSRKPNRKTNT-----SFMLQLSSALAFLHKN 158
Cdd:cd14210   81 KDS--------------------FIFRG--HLCIVFELLS---INLYELLKSNNFQGLSlslirKFAKQILQALQFLHKL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQTRLDtsdlepTLKVADFGLSkvcsasgqnpeepvsvnkCFLS----TACGTDFYMAPEVWEGH- 233
Cdd:cd14210  136 NIIHCDLKPENILLKQPSKS------SIKVIDFGSS------------------CFEGekvyTYIQSRFYRAPEVILGLp 191
                        250
                 ....*....|....
gi 119628251 234 YTAKADIFALGIII 247
Cdd:cd14210  192 YDTAIDMWSLGCIL 205
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
8-319 1.09e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 75.91  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHApenveLALREfwalssiksqhpnviHLEECILQKDgmvqKMSHG 87
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQN-----LILRN---------------QIQQVFVERD----ILTFA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNS---SLYlqlvetslkgeIAFDPRSayYLWFVMDFCDGGDMNEYLlsrkpnrKTNTSFMLQLSS--------ALAFLH 156
Cdd:cd05609   58 ENPfvvSMY-----------CSFETKR--HLCMVMEYVEGGDCATLL-------KNIGPLPVDMARmyfaetvlALEYLH 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTrldtsdlePTLKVADFGLSKVCSAS-------GQNPEEPvsvnKCFLS-TACGTDFYMAPE 228
Cdd:cd05609  118 SYGIVHRDLKPDNLLITSM--------GHIKLTDFGLSKIGLMSlttnlyeGHIEKDT----REFLDkQVCGTPEYIAPE 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 229 V--WEGhYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQgtEIvpvgeallENPKMELLIPVKKKSmngrmkq 306
Cdd:cd05609  186 VilRQG-YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD--EI--------EWPEGDDALPDDAQD------- 247
                        330
                 ....*....|...
gi 119628251 307 LIKEMLAANPQDR 319
Cdd:cd05609  248 LITRLLQQNPLER 260
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
7-325 1.16e-15

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 75.50  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapenVELALREFWalssIKSQHPNVIHLEECILQKdgmVQKMSH 86
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIF------KERILVDTW----VRDRKLGTVPLEIHILDT---LNKRSH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvETSLKGEIAFDPRSAYYLwfVMDfCDGGDMNEY-LLSRKPN--RKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14004   68 -----------PNIVKLLDFFEDDEFYYL--VME-KHGSGMDLFdFIERKPNmdEKEAKYIFRQVADAVKHLHDQGIVHR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGlSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKA-DIF 241
Cdd:cd14004  134 DIKDENVIL--------DGNGTIKLIDFG-SAAYIKSGP------------FDTFVGTIDYAAPEVLRGNpYGGKEqDIW 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERIT-FIDTEtkkellgsyvkqgtEIVpvgEALLENPKMellipVKKKSMNgrmkqLIKEMLAANPQDRP 320
Cdd:cd14004  193 ALGVLLYTLVFKENpFYNIE--------------EIL---EADLRIPYA-----VSEDLID-----LISRMLNRDVGDRP 245

                 ....*
gi 119628251 321 DAFEL 325
Cdd:cd14004  246 TIEEL 250
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
5-325 1.16e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 75.85  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHLEECILQKDGmvqkm 84
Cdd:cd06645   10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCK--HSNIVAYFGSYLRRDK----- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLS-SALAFLHKNQIIHR 163
Cdd:cd06645   83 ------------------------------LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETlQGLYYLHSKGKMHR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdlePTLKVADFGLSKVCSASgqnpeepVSVNKCFLstacGTDFYMAPEVW----EGHYTAKAD 239
Cdd:cd06645  133 DIKGANILLTDN--------GHVKLADFGVSAQITAT-------IAKRKSFI----GTPYWMAPEVAaverKGGYNQLCD 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGI--IIWAMLERITFiDTETKKELlgsYVKQGTEIVPvgeallenPKMEllipvKKKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd06645  194 IWAVGItaIELAELQPPMF-DLHPMRAL---FLMTKSNFQP--------PKLK-----DKMKWSNSFHHFVKMALTKNPK 256

                 ....*...
gi 119628251 318 DRPDAFEL 325
Cdd:cd06645  257 KRPTAEKL 264
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
7-251 1.21e-15

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 75.72  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA-----PENVElALREfwalSSIK--------SQHPNVIHLEEC 73
Cdd:cd14182    4 KYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGggsfsPEEVQ-ELRE----ATLKeidilrkvSGHPNIIQLKDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ilqkdgmvqkmshgsnsslylqlvetslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQL 148
Cdd:cd14182   79 ---------------------------------YETNTFFFL--VFDLMKKGELFDYLtekvtLSEKETRK----IMRAL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 149 SSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSkvCS-ASGQNpeepvsvnkcfLSTACGTDFYMAP 227
Cdd:cd14182  120 LEVICALHKLNIVHRDLKPENILL--------DDDMNIKLTDFGFS--CQlDPGEK-----------LREVCGTPGYLAP 178
                        250       260       270
                 ....*....|....*....|....*....|.
gi 119628251 228 EVWE-----GH--YTAKADIFALGIIIWAML 251
Cdd:cd14182  179 EIIEcsmddNHpgYGKEVDMWSTGVIMYTLL 209
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-324 1.27e-15

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 75.85  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIR-------CHAPENVELALREfwalssIKSQHPNVIHLEECilqkdgmvqkm 84
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRkrrrgqdCRNEILHEIAVLE------LCKDCPRVVNLHEV----------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 sHGSNSSLYLqLVETSLKGEIafdprsayylwfvMDFCDGGDMneylLSRKPNRKtntsFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14106   77 -YETRSELIL-ILELAAGGEL-------------QTLLDEEEC----LTEADVRR----LMRQILEGVQYLHERNIVHLD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTRLDTSdleptLKVADFGLSKVCSAsGQNPEEPVsvnkcflstacGTDFYMAPEVWegHY---TAKADIF 241
Cdd:cd14106  134 LKPQNILLTSEFPLGD-----IKLCDFGISRVIGE-GEEIREIL-----------GTPDYVAPEIL--SYepiSLATDMW 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLERITFIDTETKKellgsyvkqgteivpvgEALLENPKMELLIPVKK-KSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14106  195 SIGVLTYVLLTGHSPFGGDDKQ-----------------ETFLNISQCNLDFPEELfKDVSPLAIDFIKRLLVKDPEKRL 257

                 ....
gi 119628251 321 DAFE 324
Cdd:cd14106  258 TAKE 261
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
115-251 1.32e-15

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 76.29  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDM-----NEYLLSRKpnrktNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKV 188
Cdd:cd05582   72 LYLILDFLRGGDLftrlsKEVMFTEE-----DVKFYLaELALALDHLHSLGIIYRDLKPENILL--------DEDGHIKL 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 189 ADFGLSKvcsasgqnpEEPVSVNKCFlsTACGTDFYMAPEV--WEGHYTAkADIFALGIIIWAML 251
Cdd:cd05582  139 TDFGLSK---------ESIDHEKKAY--SFCGTVEYMAPEVvnRRGHTQS-ADWWSFGVLMFEML 191
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
10-253 1.57e-15

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 76.71  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENV---ELALREFWALSSIKsqHPNVIHLEECilqkdgmvqkmsh 86
Cdd:cd07853    4 PDRPIGYGAFGVVWSVTDPRDGKRVALKKMP-NVFQNLvscKRVFRELKMLCFFK--HDNVLSALDI------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslyLQLVETSLKGEIafdprsaYYLWFVMDfcdgGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07853   68 -------LQPPHIDPFEEI-------YVVTELMQ----SDLHKIIVSPQPLSSDHVKvFLYQILRGLKYLHSAGILHRDI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISqtrldtSDLepTLKVADFGLSKVcsasgQNPEEpvsvnKCFLSTACGTDFYMAPEVWEG--HYTAKADIFAL 243
Cdd:cd07853  130 KPGNLLVN------SNC--VLKICDFGLARV-----EEPDE-----SKHMTQEVVTQYYRAPEILMGsrHYTSAVDIWSV 191
                        250
                 ....*....|
gi 119628251 244 GIIIWAMLER 253
Cdd:cd07853  192 GCIFAELLGR 201
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
13-248 1.96e-15

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 74.97  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElalREFWALSSIKSQ--HPNVIHLEECILQKDgmvqkmshgsns 90
Cdd:cd05084    3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLK---AKFLQEARILKQysHPNIVRLIGVCTQKQ------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdPrsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd05084   68 ------------------P-----IYIVMELVQGGDFLTFLRTEGPRLKVKEliRMVENAAAGMEYLESKHCIHRDLAAR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQtrldtsdlEPTLKVADFGLSK-----VCSASGQNPEEPVSvnkcflstacgtdfYMAPEVWE-GHYTAKADIFA 242
Cdd:cd05084  125 NCLVTE--------KNVLKISDFGMSReeedgVYAATGGMKQIPVK--------------WTAPEALNyGRYSSESDVWS 182

                 ....*.
gi 119628251 243 LGIIIW 248
Cdd:cd05084  183 FGILLW 188
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
14-321 2.01e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 75.07  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIR-------CHAPENVELALREFWALSsiksqHPNVIHLEECILQKDGmvqkmsh 86
Cdd:cd14147   11 IGIGGFGKVYRGSWR--GELVAVKAARqdpdediSVTAESVRQEARLFAMLA-----HPNIIALKAVCLEEPN------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQI---IHR 163
Cdd:cd14147   77 ----------------------------LCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHR 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTAcGTDFYMAPEVWEGHYTAK-ADIFA 242
Cdd:cd14147  129 DLKSNNILLLQPIENDDMEHKTLKITDFGLAREWHKTTQ------------MSAA-GTYAWMAPEVIKASTFSKgSDVWS 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 243 LGIIIWAMLEritfidtetkkellGSYVKQGTEIVPVGEALLENpKMELLIPvkkKSMNGRMKQLIKEMLAANPQDRPD 321
Cdd:cd14147  196 FGVLLWELLT--------------GEVPYRGIDCLAVAYGVAVN-KLTLPIP---STCPEPFAQLMADCWAQDPHRRPD 256
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
8-252 2.09e-15

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 75.43  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEnvelalrefwalssiksqhpnvihlEECILQKDGMVQKMSHG 87
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE-------------------------EEEIKLEINMLKKYSHH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SN-SSLYLQLVETSLKGEiafDPRsayyLWFVMDFCDGGDMNEYLLSRKPN--RKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd06636   73 RNiATYYGAFIKKSPPGH---DDQ----LWLVMEFCGAGSVTDLVKNTKGNalKEDWIAYICrEILRGLAHLHAHKVIHR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdlePTLKVADFGLSKvcsasgqNPEEPVSVNKCFLstacGTDFYMAPEVW------EGHYTAK 237
Cdd:cd06636  146 DIKGQNVLLTEN--------AEVKLVDFGVSA-------QLDRTVGRRNTFI----GTPYWMAPEVIacdenpDATYDYR 206
                        250
                 ....*....|....*
gi 119628251 238 ADIFALGIIIWAMLE 252
Cdd:cd06636  207 SDIWSLGITAIEMAE 221
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
7-324 2.42e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 77.08  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALrEFWALSSIKsqHPNVIHLEECILQKdgmvqk 83
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGlkeREKSQLVI-EVNVMRELK--HKNIVRYIDRFLNK------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   84 mshgSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNE-----YLLSRKPNRKTNTSFMLQLSSALAFLHK- 157
Cdd:PTZ00266   85 ----ANQKLYI-----------------------LMEFCDAGDLSRniqkcYKMFGKIEEHAIVDITRQLLHALAYCHNl 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  158 ------NQIIHRDLKPDNILIS---------QTRLDTSDLEPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTAC-GT 221
Cdd:PTZ00266  138 kdgpngERVLHRDLKPQNIFLStgirhigkiTAQANNLNGRPIAKIGDFGLSK-------------NIGIESMAHSCvGT 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  222 DFYMAPEVW---EGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEivpvgeallenpkmellIPVKKK 298
Cdd:PTZ00266  205 PYYWSPELLlheTKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQLISELKRGPD-----------------LPIKGK 267
                         330       340
                  ....*....|....*....|....*.
gi 119628251  299 SMngRMKQLIKEMLAANPQDRPDAFE 324
Cdd:PTZ00266  268 SK--ELNILIKNLLNLSAKERPSALQ 291
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
12-266 2.43e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 74.96  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REV-GRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGMVqkmshgsns 90
Cdd:cd14190    9 KEVlGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQL--NHRNLIQLYEAIETPNEIV--------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRK-PNRKTNTS-FMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd14190   78 --------------------------LFMEYVEGGELFERIVDEDyHLTEVDAMvFVRQICEGIQFMHQMRVLHLDLKPE 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTrldTSDLeptLKVADFGLskvcsASGQNPEEPVSVNkcflstaCGTDFYMAPEVWEGHYTA-KADIFALGIII 247
Cdd:cd14190  132 NILCVNR---TGHQ---VKIIDFGL-----ARRYNPREKLKVN-------FGTPEFLSPEVVNYDQVSfPTDMWSMGVIT 193
                        250       260
                 ....*....|....*....|...
gi 119628251 248 WAMLERIT-FI---DTETKKELL 266
Cdd:cd14190  194 YMLLSGLSpFLgddDTETLNNVL 216
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
119-247 3.01e-15

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 74.77  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNE-YLLSRKPNRKTNTSFMLQLS----SALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd06621   80 MEYCEGGSLDSiYKKVKKKGGRIGEKVLGKIAesvlKGLSYLHSRKIIHRDIKPSNILL--------TRKGQVKLCDFGV 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 194 skvcsaSGQnpeepvSVNKcFLSTACGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd06621  152 ------SGE------LVNS-LAGTFTGTSYYMAPERIQGGpYSITSDVWSLGLTL 193
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
74-324 3.08e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 75.43  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDGMVQK--MSHGSNSSLYLQLVE----TSLKgeIAFDPRSAyyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-L 146
Cdd:cd05595   27 ILRKEVIIAKdeVAHTVTESRVLQNTRhpflTALK--YAFQTHDR--LCFVMEYANGGELFFHLSRERVFTEDRARFYgA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSvNKCFLSTACGTDFYMA 226
Cdd:cd05595  103 EIVSALEYLHSRDVVYRDIKLENLML--------DKDGHIKITDFGLCK----------EGIT-DGATMKTFCGTPEYLA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 227 PEVWEGH-YTAKADIFALGIIIWAML-ERITFIDTETKKELlgsyvkqgtEIVPVGEalLENPKMelLIPVKKKSMNGRM 304
Cdd:cd05595  164 PEVLEDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHERLF---------ELILMEE--IRFPRT--LSPEAKSLLAGLL 230
                        250       260
                 ....*....|....*....|
gi 119628251 305 KQLIKEMLAANPQDRPDAFE 324
Cdd:cd05595  231 KKDPKQRLGGGPSDAKEVME 250
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
8-251 3.47e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 75.03  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPENVELALRE---FWALSSikSQHPNVIHLEECILQKDgmv 81
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKalkKGDIIARDEVESLMCEkriFETVNS--ARHPFLVNLFACFQTPE--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMneyllsrkpnrktntsfMLQLSS----------- 150
Cdd:cd05589   76 --------------------------------HVCFVMEYAAGGDL-----------------MMHIHEdvfsepravfy 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ------ALAFLHKNQIIHRDLKPDNILisqtrLDTsdlEPTLKVADFGLSKVCSASGQNPeepvsvnkcflSTACGTDFY 224
Cdd:cd05589  107 aacvvlGLQFLHEHKIVYRDLKLDNLL-----LDT---EGYVKIADFGLCKEGMGFGDRT-----------STFCGTPEF 167
                        250       260
                 ....*....|....*....|....*...
gi 119628251 225 MAPEVW-EGHYTAKADIFALGIIIWAML 251
Cdd:cd05589  168 LAPEVLtDTSYTRAVDWWGLGVLIYEML 195
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
14-254 3.59e-15

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 74.47  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEaVIRKTSARVAVKK--IRCHApENVELALREFWALSSIksQHPNVIHLEEcILQKDGMvqkmshgsnss 91
Cdd:cd14154    1 LGKGFFGQAIK-VTHRETGEVMVMKelIRFDE-EAQRNFLKEVKVMRSL--DHPNVLKFIG-VLYKDKK----------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYL--LSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd14154   65 -----------------------LNLITEYIPGGTLKDVLkdMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISQTRldtsdlepTLKVADFGLSKVCSASGQNPEEPVSVNKCFLS---------TACGTDFYMAPEVWEGH-YTAKAD 239
Cdd:cd14154  122 CLVREDK--------TVVVADFGLARLIVEERLPSGNMSPSETLRHLkspdrkkryTVVGNPYWMAPEMLNGRsYDEKVD 193
                        250
                 ....*....|....*
gi 119628251 240 IFALGIIIWAMLERI 254
Cdd:cd14154  194 IFSFGIVLCEIIGRV 208
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
74-251 3.79e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 75.09  E-value: 3.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDGMVQK--MSHGSNSSLYLQLVE----TSLKgeIAFdpRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-L 146
Cdd:cd05571   27 ILKKEVIIAKdeVAHTLTENRVLQNTRhpflTSLK--YSF--QTNDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYgA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSVNKCfLSTACGTDFYMA 226
Cdd:cd05571  103 EIVLALGYLHSQGIVYRDLKLENLLL--------DKDGHIKITDFGLCK----------EEISYGAT-TKTFCGTPEYLA 163
                        170       180
                 ....*....|....*....|....*.
gi 119628251 227 PEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05571  164 PEVLEDNdYGRAVDWWGLGVVMYEMM 189
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
10-251 4.32e-15

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 74.30  E-value: 4.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAV---IRKTSA--RVAVKKIRchapENVELALR-EFWALSSIKSQH--PNVIHLEecilqkdGMV 81
Cdd:cd05032   10 LIRELGQGSFGMVYEGLakgVVKGEPetRVAIKTVN----ENASMRERiEFLNEASVMKEFncHHVVRLL-------GVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMSHgsnsslylQLVetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNTSFM-----------LQLSS 150
Cdd:cd05032   79 STGQP--------TLV--------------------VMELMAKGDLKSYLRSRRPEAENNPGLGpptlqkfiqmaAEIAD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ALAFLHKNQIIHRDLKPDNILISqtrldtSDLepTLKVADFGLSKvcsasgqnpeepvSVNKcflstacgTDFY------ 224
Cdd:cd05032  131 GMAYLAAKKFVHRDLAARNCMVA------EDL--TVKIGDFGMTR-------------DIYE--------TDYYrkggkg 181
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119628251 225 ------MAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05032  182 llpvrwMAPEsLKDGVFTTKSDVWSFGVVLWEMA 215
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-321 5.89e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 73.91  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIrchapenvelalrEFWALSSIKSQhpnvihlEECIlQKDGMVQKMSHgSNSS 91
Cdd:cd08228    8 KKIGRGQFSEVYRATCLLDRKPVALKKV-------------QIFEMMDAKAR-------QDCV-KEIDLLKQLNH-PNVI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 LYL-QLVETSlkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRK-----TNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd08228   66 KYLdSFIEDN-------------ELNIVLELADAGDLSQMIKYFKKQKRliperTVWKYFVQLCSAVEHMHSRRVMHRDI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPE-VWEGHYTAKADIFALG 244
Cdd:cd08228  133 KPANVFITATGV--------VKLGDLGLGRFFSSKTTAAHSLV-----------GTPYYMSPErIHENGYNFKSDIWSLG 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 245 IIIWAMleritfidtetkkellgsyvkqgteivpvgeALLENP----KMELLI-----------PVKKKSMNGRMKQLIK 309
Cdd:cd08228  194 CLLYEM-------------------------------AALQSPfygdKMNLFSlcqkieqcdypPLPTEHYSEKLRELVS 242
                        330
                 ....*....|..
gi 119628251 310 EMLAANPQDRPD 321
Cdd:cd08228  243 MCIYPDPDQRPD 254
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
8-319 6.13e-15

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 74.67  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRK---TSARVAVKKIRCHAPENVELALREFWALSSiKSQHPNVIHLEECIlqkdgmvqkm 84
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKndqIYAMKVVKKELVHDDEDIDWVQTEKHVFEQ-ASSNPFLVGLHSCF---------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdpRSAYYLWFVMDFCDGGDMNEYLL-SRKPNRKTNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05617   86 -------------------------QTTSRLFLVIEYVNGGDLMFHMQrQRKLPEEHARFYAAEICIALNFLHERGIIYR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsaSGQNPEEPVsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05617  141 DLKLDNVLL--------DADGHIKLTDYGMCK----EGLGPGDTT-------STFCGTPNYIAPEILRGEeYGFSVDWWA 201
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 243 LGIIIWAMLERITFIDTETKKELLGS--YVKQgteivpvgeALLENPkmeLLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd05617  202 LGVLMFEMMAGRSPFDIITDNPDMNTedYLFQ---------VILEKP---IRIP---RFLSVKASHVLKGFLNKDPKER 265
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
8-325 6.82e-15

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 73.98  E-value: 6.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEnvelalrefwalssiksqhpnvihlEECILQKDGMVQKMSHG 87
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDE-------------------------EEEIKQEINMLKKYSHH 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SN-SSLYLQLVETSLKGeiaFDPRsayyLWFVMDFCDGGDMNEYLLSRKPN--RKTNTSFML-QLSSALAFLHKNQIIHR 163
Cdd:cd06637   63 RNiATYYGAFIKKNPPG---MDDQ----LWLVMEFCGAGSVTDLIKNTKGNtlKEEWIAYICrEILRGLSHLHQHKVIHR 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdlePTLKVADFGLSKvcsasgqNPEEPVSVNKCFLstacGTDFYMAPEVW------EGHYTAK 237
Cdd:cd06637  136 DIKGQNVLLTEN--------AEVKLVDFGVSA-------QLDRTVGRRNTFI----GTPYWMAPEVIacdenpDATYDFK 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 ADIFALGIIIWAMleritfidTETKKELLGSYVKQGTEIVPvgeallENPKMELlipvKKKSMNGRMKQLIKEMLAANPQ 317
Cdd:cd06637  197 SDLWSLGITAIEM--------AEGAPPLCDMHPMRALFLIP------RNPAPRL----KSKKWSKKFQSFIESCLVKNHS 258

                 ....*...
gi 119628251 318 DRPDAFEL 325
Cdd:cd06637  259 QRPSTEQL 266
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-251 7.00e-15

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 73.41  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   4 SQPKYDLIREVGRGSYGVVYEAViRKTSARVAVKKIRCHAPENVELALREFWALSSIKsqHPNVIHLEECILqkdgmvqk 83
Cdd:cd14110    1 TEKTYAFQTEINRGRFSVVRQCE-EKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLS--HPRIAQLHSAYL-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnSSLYLQLVEtslkgeiafdprsayylwfvmDFCDGGDMNEYLLSRKPNRKTN-TSFMLQLSSALAFLHKNQIIH 162
Cdd:cd14110   70 ------SPRHLVLIE---------------------ELCSGPELLYNLAERNSYSEAEvTDYLWQILSAVDYLHSRRILH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLdtsdleptLKVADFGlskvcSASGQNPEEPVSVNKC--FLSTacgtdfyMAPEVWEGH-YTAKAD 239
Cdd:cd14110  123 LDLRSENMIITEKNL--------LKIVDLG-----NAQPFNQGKVLMTDKKgdYVET-------MAPELLEGQgAGPQTD 182
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd14110  183 IWAIGVTAFIML 194
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
8-264 7.98e-15

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 73.07  E-value: 7.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN--VELALREFWALSSiKSQHPNVIHLeecilqkdgmvqkms 85
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKagVEHQLRREVEIQS-HLRHPNILRL--------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGsnsslYLQlvetslkgeiafdprSAYYLWFVMDFCDGGDMNEYL--LSRKPNRKTNTsFMLQLSSALAFLHKNQIIHR 163
Cdd:cd14116   71 YG-----YFH---------------DATRVYLILEYAPLGTVYRELqkLSKFDEQRTAT-YITELANALSYCHSKRVIHR 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldtSDLEptLKVADFGLSKVCSASGQnpeepvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd14116  130 DIKPENLLLG------SAGE--LKIADFGWSVHAPSSRR-------------TTLCGTLDYLPPEMIEGRmHDEKVDLWS 188
                        250       260
                 ....*....|....*....|..
gi 119628251 243 LGIIIWAMLERITFIDTETKKE 264
Cdd:cd14116  189 LGVLCYEFLVGKPPFEANTYQE 210
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
13-319 8.25e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 73.55  E-value: 8.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHApenvelALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHG 87
Cdd:cd14118    1 EIGKGSYGIVKLAYNEEDNTLYAMKilskkKLLKQA------GFFRRPPPRRKPGALGKPLDPLDRVYREIAILKKLDHP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SnsslYLQLVEtslkgeIAFDPRSAYyLWFVMDFCDGGDMNEyLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd14118   75 N----VVKLVE------VLDDPNEDN-LYMVFELVDKGAVME-VPTDNPlSEETARSYFRDIVLGIEYLHYQKIIHRDIK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQtrldtsdlEPTLKVADFGLSkvCSASGqnpeepvsvNKCFLSTACGTDFYMAPEVWEG---HYTAKA-DIFA 242
Cdd:cd14118  143 PSNLLLGD--------DGHVKIADFGVS--NEFEG---------DDALLSSTAGTPAFMAPEALSEsrkKFSGKAlDIWA 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 243 LGIIIWAML-ERITFIDTetkkELLGSYVKQGTEivpvgeallenpkmELLIPvKKKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14118  204 MGVTLYCFVfGRCPFEDD----HILGLHEKIKTD--------------PVVFP-DDPVVSEQLKDLILRMLDKNPSER 262
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
8-268 8.49e-15

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 73.51  E-value: 8.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI---------RCHAPENVElalREFWALSSIksQHPNVIHLEECILQKD 78
Cdd:cd14194    7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIkkrrtkssrRGVSREDIE---REVSILKEI--QHPNVITLHEVYENKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 GMVqkmshgsnssLYLQLVEtslkgeiafdprsayylwfvmdfcdGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHK 157
Cdd:cd14194   82 DVI----------LILELVA-------------------------GGELFDFLAEKESlTEEEATEFLKQILNGVYYLHS 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWegHYTA- 236
Cdd:cd14194  127 LQIAHFDLKPENIML----LDRNVPKPRIKIIDFGLAHKIDFGNE------------FKNIFGTPEFVAPEIV--NYEPl 188
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119628251 237 --KADIFALGIIIWAMLERITFIDTETKKELLGS 268
Cdd:cd14194  189 glEADMWSIGVITYILLSGASPFLGDTKQETLAN 222
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
14-320 8.68e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 73.15  E-value: 8.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIRCHAPENVELA---LREFWALSSIKsQHPNVIHLEECILQKDgmvqkmshgsns 90
Cdd:cd14146    2 IGVGGFGKVYRATWK--GQEVAVKAARQDPDEDIKATaesVRQEAKLFSML-RHPNIIKLEGVCLEEP------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLS----------RKPNRKTNTSFMLQLSSALAFLHKNQ- 159
Cdd:cd14146   67 -----------------------NLCLVMEFARGGTLNRALAAanaapgprraRRIPPHILVNWAVQIARGMLYLHEEAv 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 --IIHRDLKPDNILISQtRLDTSDL-EPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTACGTDFYMAPEVWEGHYTA 236
Cdd:cd14146  124 vpILHRDLKSSNILLLE-KIEHDDIcNKTLKITDFGLAR-------------EWHRTTKMSAAGTYAWMAPEVIKSSLFS 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 K-ADIFALGIIIWAMLEritfidtetkkellGSYVKQGTEIVPVGEALLENpKMELLIPvkkKSMNGRMKQLIKEMLAAN 315
Cdd:cd14146  190 KgSDIWSYGVLLWELLT--------------GEVPYRGIDGLAVAYGVAVN-KLTLPIP---STCPEPFAKLMKECWEQD 251

                 ....*
gi 119628251 316 PQDRP 320
Cdd:cd14146  252 PHIRP 256
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
115-251 9.31e-15

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 73.89  E-value: 9.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-LQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05575   71 LYFVLDYVNGGELFFHLQRERHFPEPRARFYaAEIASALGYLHSLNIIYRDLKPENILL--------DSQGHVVLTDFGL 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 194 SKvcsaSGQNPEEPVsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05575  143 CK----EGIEPSDTT-------STFCGTPEYLAPEVLRKQpYDRTVDWWCLGAVLYEML 190
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
8-266 9.45e-15

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 73.29  E-value: 9.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVA---VKKIRCHAP------ENVElalREFWALSSIksQHPNVIHLEECILQKD 78
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASrrgvsrEDIE---REVSILRQV--LHPNIITLHDVFENKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 GMVqkmshgsnssLYLQLVEtslkgeiafdprsayylwfvmdfcdGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHK 157
Cdd:cd14105   82 DVV----------LILELVA-------------------------GGELFDFLAEKESlSEEEATEFLKQILDGVNYLHT 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEV--WEGhYT 235
Cdd:cd14105  127 KNIAHFDLKPENIML----LDKNVPIPRIKLIDFGLAHKIEDGNE------------FKNIFGTPEFVAPEIvnYEP-LG 189
                        250       260       270
                 ....*....|....*....|....*....|.
gi 119628251 236 AKADIFALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14105  190 LEADMWSIGVITYILLSGASPFLGDTKQETL 220
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
15-248 1.01e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 73.25  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKirCHAPENVELALREFWALS-SI--KSQHPNVIhlEECILQKDGMVQKMSHgsnss 91
Cdd:cd13989    2 GSGGFGYVTLWKHQDTGEYVAIKK--CRQELSPSDKNRERWCLEvQImkKLNHPNVV--SARDVPPELEKLSPND----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lyLQLVetslkgeiafdprsayylwfVMDFCDGGDMNEYLlsrkpNRKTNTSFMLQ---------LSSALAFLHKNQIIH 162
Cdd:cd13989   73 --LPLL--------------------AMEYCSGGDLRKVL-----NQPENCCGLKEsevrtllsdISSAISYLHENRIIH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLDTsdlepTLKVADFGLSKVCSASgqnpeepvSVNKCFLstacGTDFYMAPEVWEGH-YTAKADIF 241
Cdd:cd13989  126 RDLKPENIVLQQGGGRV-----IYKLIDLGYAKELDQG--------SLCTSFV----GTLQYLAPELFESKkYTCTVDYW 188

                 ....*..
gi 119628251 242 ALGIIIW 248
Cdd:cd13989  189 SFGTLAF 195
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
8-325 1.13e-14

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 72.69  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHaPENVELALREFWALS----SIKSQHPNVIHLEECILQKDgmvqk 83
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNN-KDYLDQSLDEIRLLEllnkKDKADKYHIVRLKDVFYFKN----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslYLQLVETSLKgeiafdprsayylwfvmdfcdggdMNEYLLSRKpNRKTNTS------FMLQLSSALAFLHK 157
Cdd:cd14133   75 ---------HLCIVFELLS------------------------QNLYEFLKQ-NKFQYLSlprirkIAQQILEALVFLHS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQTRldtsdlEPTLKVADFGLSkvcsasgqnpeepvsvnkCFLSTACGT----DFYMAPEVWEG- 232
Cdd:cd14133  121 LGLIHCDLKPENILLASYS------RCQIKIIDFGSS------------------CFLTQRLYSyiqsRYYRAPEVILGl 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 HYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVkqgteivpvgeALLENPKMELLipvkKKSMNGR--MKQLIKE 310
Cdd:cd14133  177 PYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARII-----------GTIGIPPAHML----DQGKADDelFVDFLKK 241
                        330
                 ....*....|....*
gi 119628251 311 MLAANPQDRPDAFEL 325
Cdd:cd14133  242 LLEIDPKERPTASQA 256
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
110-319 1.19e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 72.71  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 110 RSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTN---TSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTsdlepTL 186
Cdd:cd14172   71 HGKRCLLIIMECMEGGELFSRIQERGDQAFTEreaSEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDA-----VL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 187 KVADFGLSKvcSASGQNPeepvsvnkcfLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAMLERITFIDTETkkel 265
Cdd:cd14172  146 KLTDFGFAK--ETTVQNA----------LQTPCYTPYYVAPEVLgPEKYDKSCDMWSLGVIMYILLCGFPPFYSNT---- 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 266 lGSYVKQGTEI-VPVGEALLENPKMellipvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14172  210 -GQAISPGMKRrIRMGQYGFPNPEW--------AEVSEEAKQLIRHLLKTDPTER 255
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
7-279 1.32e-14

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 73.78  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrcHAPENVEL-ALREFWALSSIKS-QHPNVIHLeecilqKDGMVQKM 84
Cdd:cd07879   16 RYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKL--SRPFQSEIfAKRAYRELTLLKHmQHENVIGL------LDVFTSAV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLQLvetslkgeiafdPRSAYYLWFVMDFCDGGDMNEYLLsrkpnrktntsfmLQLSSALAFLHKNQIIHRD 164
Cdd:cd07879   88 SGDEFQDFYLVM------------PYMQTDLQKIMGHPLSEDKVQYLV-------------YQMLCGLKYIHSAGIIHRD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQtrldtsDLEptLKVADFGLSKVCSASgqnpeepvsvnkcfLSTACGTDFYMAPEV---WEgHYTAKADIF 241
Cdd:cd07879  143 LKPGNLAVNE------DCE--LKILDFGLARHADAE--------------MTGYVVTRWYRAPEVilnWM-HYNQTVDIW 199
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 119628251 242 ALGIIIWAMLERITFIDTEtkkellgSYVKQGTEIVPV 279
Cdd:cd07879  200 SVGCIMAEMLTGKTLFKGK-------DYLDQLTQILKV 230
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
10-328 1.43e-14

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 72.68  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKTSaRVAVKKIRchapenvELALREfwalssiksqhpnvihlEECILQKDGMVqKMSHGSN 89
Cdd:cd05112    8 FVQEIGSGQFGLVHLGYWLNKD-KVAIKTIR-------EGAMSE-----------------EDFIEEAEVMM-KLSHPKL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 SSLYLQLVEtslkgeiafdpRSAYYLwfVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd05112   62 VQLYGVCLE-----------QAPICL--VFEFMEHGCLSDYLRTQRGlfSAETLLGMCLDVCEGMAYLEEASVIHRDLAA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQTRLdtsdleptLKVADFGLSKVcsasgqnpeepvsVNKCFLSTACGTDF---YMAPEVWE-GHYTAKADIFAL 243
Cdd:cd05112  129 RNCLVGENQV--------VKVSDFGMTRF-------------VLDDQYTSSTGTKFpvkWSSPEVFSfSRYSSKSDVWSF 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 244 GIIIWAML-ERITFIDTETKKELLgsyvkqgtEIVPVGEALLEnPKMellipvKKKSMNGRMKQLIKEmlaaNPQDRPdA 322
Cdd:cd05112  188 GVLMWEVFsEGKIPYENRSNSEVV--------EDINAGFRLYK-PRL------ASTHVYEIMNHCWKE----RPEDRP-S 247

                 ....*.
gi 119628251 323 FELELR 328
Cdd:cd05112  248 FSLLLR 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
14-251 1.44e-14

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 72.14  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIRchapENVELALREFWALssiksQHPNVIhleecilqkdgmvqkmshgsnssly 93
Cdd:cd14059    1 LGSGAQGAVFLGKFR--GEEVAVKKVR----DEKETDIKHLRKL-----NHPNII------------------------- 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetSLKGEIAFDPrsAYYLwfVMDFCDGGDMNEYLLSRKPNRKTN-TSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14059   45 ------KFKGVCTQAP--CYCI--LMEYCPYGQLYEVLRAGREITPSLlVDWSKQIASGMNYLHLHKIIHRDLKSPNVLV 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvSVNKCFlstaCGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd14059  115 TY--------NDVLKISDFGTSKELSEK--------STKMSF----AGTVAWMAPEVIRNEpCSEKVDIWSFGVVLWELL 174
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
13-325 1.65e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 73.10  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIhleecilqkdgmvqkmshgsnssl 92
Cdd:cd06659   28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDY--QHPNVV------------------------ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylQLVETSLKGEiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd06659   82 --EMYKSYLVGE---------ELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SqtrldtsdLEPTLKVADFGLskvCSASGQNPEEPVSVnkcflstaCGTDFYMAPEV-WEGHYTAKADIFALGIIIWAML 251
Cdd:cd06659  151 T--------LDGRVKLSDFGF---CAQISKDVPKRKSL--------VGTPYWMAPEViSRCPYGTEVDIWSLGIMVIEMV 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 252 --ERITFIDT--ETKKELLGS---YVKQGTEIVPVgeallenpkmellipvkkksmngrMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd06659  212 dgEPPYFSDSpvQAMKRLRDSpppKLKNSHKASPV------------------------LRDFLERMLVRDPQERATAQE 267

                 .
gi 119628251 325 L 325
Cdd:cd06659  268 L 268
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
8-272 1.85e-14

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 73.11  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA---PENVELALREFWALSsIKSQHPNVIHLEECIlqkdgmvQKM 84
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVviqDDDVECTMVEKRVLA-LSGKPPFLTQLHSCF-------QTM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHR 163
Cdd:cd05616   74 DR----------------------------LYFVMEYVNGGDLMYHIQQVGRFKEPHAVFyAAEIAIGLFFLQSKGIIYR 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgQNPEEPVSVNkcflsTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd05616  126 DLKLDNVML--------DSEGHIKIADFGMCK------ENIWDGVTTK-----TFCGTPDYIAPEIIAYQpYGKSVDWWA 186
                        250       260       270
                 ....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLERITFIDTETKKELLGSYVKQ 272
Cdd:cd05616  187 FGVLLYEMLAGQAPFEGEDEDELFQSIMEH 216
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
115-247 1.87e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 72.28  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISqtrldtsdLEPTLKVADFGL 193
Cdd:cd14222   65 LNLLTEFIEGGTLKDFLRADDPfPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIK--------LDKTVVVADFGL 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 194 SKVCSASGQNP--EEPVSVNKCFLS-------TACGTDFYMAPEVWEG-HYTAKADIFALGIII 247
Cdd:cd14222  137 SRLIVEEKKKPppDKPTTKKRTLRKndrkkryTVVGNPYWMAPEMLNGkSYDEKVDIFSFGIVL 200
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
12-248 1.90e-14

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 72.09  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElalREFWALSSIKSQ--HPNVIHLEECILQKdgmvqkmshgsn 89
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLK---RKFLQEARILKQydHPNIVKLIGVCVQK------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sslylqlvetslkgeiafdprsaYYLWFVMDFCDGGDMNEYLlsRKPNRKTNTSFMLQLS----SALAFLHKNQIIHRDL 165
Cdd:cd05041   66 -----------------------QPIMIVMELVPGGSLLTFL--RKKGARLTVKQLLQMCldaaAGMEYLESKNCIHRDL 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSK-----VCSASGQNPEEPVSvnkcflstacgtdfYMAPEVWE-GHYTAKAD 239
Cdd:cd05041  121 AARNCLVGE--------NNVLKISDFGMSReeedgEYTVSDGLKQIPIK--------------WTAPEALNyGRYTSESD 178

                 ....*....
gi 119628251 240 IFALGIIIW 248
Cdd:cd05041  179 VWSFGILLW 187
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
13-322 2.14e-14

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 72.91  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSygvvyEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHL-----EECILQKDGMVqkmshg 87
Cdd:cd14018   26 SAGSSS-----EAILRSMGNELVPAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVqraftDSVPLLPGAIE------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snssLYLQLVETSLKGEIAFDPRSAYYLWFVMDFcdggDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd14018   95 ----DYPDVLPARLNPSGLGHNRTLFLVMKNYPC----TLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtRLDtSDLEPTLKVADFGLSKVCSASG-QNPEEPVSVNKcflstaCGTDFYMAPEVweghYTA---------- 236
Cdd:cd14018  167 DNILL---ELD-FDGCPWLVIADFGCCLADDSIGlQLPFSSWYVDR------GGNACLMAPEV----STAvpgpgvviny 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 -KADIFALGIIIWamleritfidtetkkELLGsyvkQGTEIVPVGEALLENPK-MELLIPVKKKSMNGRMKQLIKEMLAA 314
Cdd:cd14018  233 sKADAWAVGAIAY---------------EIFG----LSNPFYGLGDTMLESRSyQESQLPALPSAVPPDVRQVVKDLLQR 293

                 ....*...
gi 119628251 315 NPQDRPDA 322
Cdd:cd14018  294 DPNKRVSA 301
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
115-272 2.18e-14

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 73.11  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05615   86 LYFVMEYVNGGDLMYHIQQVGKFKEPQAVFyAAEISVGLFFLHKKGIIYRDLKLDNVML--------DSEGHIKIADFGM 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 SKvcsasgQNPEEPVSVNkcflsTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQ 272
Cdd:cd05615  158 CK------EHMVEGVTTR-----TFCGTPDYIAPEIIAYQpYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEH 226
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
13-252 2.19e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 72.38  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDgmvqkmshgsnssl 92
Cdd:cd06658   29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDY--HHENVVDMYNSYLVGD-------------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd06658   93 ---------------------ELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 sqtrldTSDlePTLKVADFGLskVCSASGQNPEEPVSVnkcflstacGTDFYMAPEVWEG-HYTAKADIFALGIIIWAML 251
Cdd:cd06658  152 ------TSD--GRIKLSDFGF--CAQVSKEVPKRKSLV---------GTPYWMAPEVISRlPYGTEVDIWSLGIMVIEMI 212

                 .
gi 119628251 252 E 252
Cdd:cd06658  213 D 213
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
114-325 2.33e-14

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 71.89  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCdggdMNEYLLSRKPNRKTNTS-----FMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsDLEptLKV 188
Cdd:cd14187   81 FVYVVLELC----RRRSLLELHKRRKALTEpearyYLRQIILGCQYLHRNRVIHRDLKLGNLFLND------DME--VKI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 189 ADFGLSKVCSASGQNPEepvsvnkcflsTACGTDFYMAPEVW--EGHyTAKADIFALGIIIWAMLERITFIDTETKKEll 266
Cdd:cd14187  149 GDFGLATKVEYDGERKK-----------TLCGTPNYIAPEVLskKGH-SFEVDIWSIGCIMYTLLVGKPPFETSCLKE-- 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 267 gSYVKQgteivpvgeallenPKMELLIPvkkKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14187  215 -TYLRI--------------KKNEYSIP---KHINPVAASLIQKMLQTDPTARPTINEL 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
118-320 2.66e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 71.76  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVC 197
Cdd:cd14027   69 VMEYMEKGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILV--------DNDFHIKIADLGLASFK 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 198 SASGQNPEEPVSVNKcfLSTAC----GTDFYMAPEvwegHY-------TAKADIFALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14027  141 MWSKLTKEEHNEQRE--VDGTAkknaGTLYYMAPE----HLndvnakpTEKSDVYSFAIVLWAIFANKEPYENAINEDQI 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119628251 267 GSYVKQGteivpvgeallENPKMELLIPVKKKSMNGRMKQLIKemlaANPQDRP 320
Cdd:cd14027  215 IMCIKSG-----------NRPDVDDITEYCPREIIDLMKLCWE----ANPEARP 253
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
10-333 2.66e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 72.03  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVV----YEAVIRKTSARVAVKKIRCHAPENVELAL-REFWALSSIksQHPNVIHLEecilqkdGMVQKM 84
Cdd:cd05038    8 FIKQLGEGHFGSVelcrYDPLGDNTGEQVAVKSLQPSGEEQHMSDFkREIEILRTL--DHEYIVKYK-------GVCESP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSnsslyLQLVetslkgeiafdprsayylwfvMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd05038   79 GRRS-----LRLI---------------------MEYLPSGSLRDYLQRHRDqiDLKRLLLFASQICKGMEYLGSQRYIH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSAS-----GQNPEE-PVsvnkcflstacgtdFYMAPE-VWEGHYT 235
Cdd:cd05038  133 RDLAARNILV--------ESEDLVKISDFGLAKVLPEDkeyyyVKEPGEsPI--------------FWYAPEcLRESRFS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAMLeriTFIDTetkkellgSYVKQGTEIVPVGEALLENPKMELLIPVKKksmNGRMKQ--------- 306
Cdd:cd05038  191 SASDVWSFGVTLYELF---TYGDP--------SQSPPALFLRMIGIAQGQMIVTRLLELLKS---GERLPRppscpdevy 256
                        330       340
                 ....*....|....*....|....*...
gi 119628251 307 -LIKEMLAANPQDRPDAFELELRLVQIA 333
Cdd:cd05038  257 dLMKECWEYEPQDRPSFSDLILIIDRLR 284
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
30-319 2.78e-14

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 74.11  E-value: 2.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251    30 TSARVAVKKIRCHAPENVELALReFWALSSIKSQ--HPNVIHLEECILQKDGMvqkmshgsnsslylqlvetslkgeiaf 107
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRAR-FRRETALCARlyHPNIVALLDSGEAPPGL--------------------------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   108 dprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNT-SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTrldtsDLEPTL 186
Cdd:TIGR03903   54 -------LFAVFEYVPGRTLREVLAADGALPAGETgRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQT-----GVRPHA 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   187 KVADFGLSKVCSASGQNPEEPVSVNKCFLstacGTDFYMAPEVWEGH-YTAKADIFALGIIIwamLERITfidtetkkel 265
Cdd:TIGR03903  122 KVLDFGIGTLLPGVRDADVATLTRTTEVL----GTPTYCAPEQLRGEpVTPNSDLYAWGLIF---LECLT---------- 184
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251   266 lGSYVKQGTEIVPVGEALLeNPkMELLIPvkkKSMNG-RMKQLIKEMLAANPQDR 319
Cdd:TIGR03903  185 -GQRVVQGASVAEILYQQL-SP-VDVSLP---PWIAGhPLGQVLRKALNKDPRQR 233
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
8-251 3.03e-14

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 72.79  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVyEAVIRKTSARVAVKKIRchapENVELALRE----FWalssiksqhpnvihlEEcilqKDGMVQk 83
Cdd:cd05596   28 FDVIKVIGRGAFGEV-QLVRHKSTKKVYAMKLL----SKFEMIKRSdsafFW---------------EE----RDIMAH- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgSNSSLYLQLvetslkgEIAF-DPRsayYLWFVMDFCDGGD----MNEYLLSRKPNRktntSFMLQLSSALAFLHKN 158
Cdd:cd05596   83 ----ANSEWIVQL-------HYAFqDDK---YLYMVMDYMPGGDlvnlMSNYDVPEKWAR----FYTAEVVLALDAIHSM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILisqtrLDTSDlepTLKVADFGlskVCSASGQNpeepvSVNKCflSTACGTDFYMAPEVWE-----GH 233
Cdd:cd05596  145 GFVHRDVKPDNML-----LDASG---HLKLADFG---TCMKMDKD-----GLVRS--DTAVGTPDYISPEVLKsqggdGV 206
                        250
                 ....*....|....*...
gi 119628251 234 YTAKADIFALGIIIWAML 251
Cdd:cd05596  207 YGRECDWWSVGVFLYEML 224
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
74-251 3.03e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 72.74  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDGMVQKMSHG---SNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLS 149
Cdd:cd05602   39 VLQKKAILKKKEEKhimSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGELFYHLQRERCFLEPRARFyAAEIA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 150 SALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgQNPEEPVSVnkcflSTACGTDFYMAPEV 229
Cdd:cd05602  119 SALGYLHSLNIVYRDLKPENILL--------DSQGHIVLTDFGLCK------ENIEPNGTT-----STFCGTPEYLAPEV 179
                        170       180
                 ....*....|....*....|...
gi 119628251 230 WEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05602  180 LHKQpYDRTVDWWCLGAVLYEML 202
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
14-248 3.13e-14

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 71.58  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIR-KTSarVAVKKIRCHAPEnvELALReFWALSSIKSQ--HPNVIHLEECILQKDGmvqkmshgsns 90
Cdd:cd05085    4 LGKGNFGEVYKGTLKdKTP--VAVKTCKEDLPQ--ELKIK-FLSEARILKQydHPNIVKLIGVCTQRQP----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTN--TSFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd05085   68 ------------------------IYIVMELVPGGDFLSFLRKKKDELKTKqlVKFSLDAAAGMAYLESKNCIHRDLAAR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTRLdtsdleptLKVADFGLSK-----VCSASGQNpEEPVSvnkcflstacgtdfYMAPEVWE-GHYTAKADIFA 242
Cdd:cd05085  124 NCLVGENNA--------LKISDFGMSRqeddgVYSSSGLK-QIPIK--------------WTAPEALNyGRYSSESDVWS 180

                 ....*.
gi 119628251 243 LGIIIW 248
Cdd:cd05085  181 FGILLW 186
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
9-247 3.27e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 72.55  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   9 DLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELAL-REFWALSSIksQHPNVIhleECilqkdgmvqkmsHG 87
Cdd:PLN00034  77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQIcREIEILRDV--NHPNVV---KC------------HD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snssLYLQlvetslKGEIAFdprsayylwfVMDFCDGGDMNeyllsrkpNRKTNTSFML-----QLSSALAFLHKNQIIH 162
Cdd:PLN00034 140 ----MFDH------NGEIQV----------LLEFMDGGSLE--------GTHIADEQFLadvarQILSGIAYLHRRHIVH 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSAsgqnpeepvSVNKCflSTACGTDFYMAPE-----VWEGHYTAK 237
Cdd:PLN00034 192 RDIKPSNLLINSAK--------NVKIADFGVSRILAQ---------TMDPC--NSSVGTIAYMSPErintdLNHGAYDGY 252
                        250
                 ....*....|.
gi 119628251 238 A-DIFALGIII 247
Cdd:PLN00034 253 AgDIWSLGVSI 263
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
8-251 3.46e-14

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 71.43  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI-RCH-APENVELALREFWALSSiKSQHPNVIHLEEcilqkdgmvqkms 85
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfKSQiEKEGVEHQLRREIEIQS-HLRHPNILRLYN------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDM-NEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14117   74 --------------------YFHDRKRIYL--ILEYAPRGELyKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISqtrldtsdLEPTLKVADFGLSkvcsasgqnpeepVSVNKCFLSTACGTDFYMAPEVWEGH-YTAKADIFAL 243
Cdd:cd14117  132 IKPENLLMG--------YKGELKIADFGWS-------------VHAPSLRRRTMCGTLDYLPPEMIEGRtHDEKVDLWCI 190

                 ....*...
gi 119628251 244 GIIIWAML 251
Cdd:cd14117  191 GVLCYELL 198
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
144-320 3.70e-14

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 71.11  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 144 FMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsDLEptLKVADFGLSKVCSASGQNPEepvsvnkcflsTACGTDF 223
Cdd:cd14189  106 YLKQIISGLKYLHLKGILHRDLKLGNFFINE------NME--LKVGDFGLAARLEPPEQRKK-----------TICGTPN 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 224 YMAPEVW--EGHYTaKADIFALGIIIWAMLERITFIDTETKKELLgSYVKQGTEIVPVgeallenpkmellipvkkkSMN 301
Cdd:cd14189  167 YLAPEVLlrQGHGP-ESDVWSLGCVMYTLLCGNPPFETLDLKETY-RCIKQVKYTLPA-------------------SLS 225
                        170
                 ....*....|....*....
gi 119628251 302 GRMKQLIKEMLAANPQDRP 320
Cdd:cd14189  226 LPARHLLAGILKRNPGDRL 244
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
7-321 3.87e-14

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 71.11  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK---------KIRCHAPENV--ELALrefwALSSIKSQHPNVIHLEECIL 75
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKfvpksrvteWAMINGPVPVplEIAL----LLKASKPGVPGVIRLLDWYE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  76 QKDGMVQKMSHgsnsslylqlvetslkgeiafdPRSAYYLWfvmDFC-DGGDMNEYLlSRKpnrktntsFMLQLSSALAF 154
Cdd:cd14005   77 RPDGFLLIMER----------------------PEPCQDLF---DFItERGALSENL-ARI--------IFRQVVEAVRH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILISQTRLDtsdleptLKVADFGlskvcsaSGQNPEEpvSVNKCFlstaCGTDFYMAPEvWEGH- 233
Cdd:cd14005  123 CHQRGVLHRDIKDENLLINLRTGE-------VKLIDFG-------CGALLKD--SVYTDF----DGTRVYSPPE-WIRHg 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 -YTAK-ADIFALGIIIWAML-ERITFidtETKKELLGSYVKqgteivpvgeallenpkmellipvKKKSMNGRMKQLIKE 310
Cdd:cd14005  182 rYHGRpATVWSLGILLYDMLcGDIPF---ENDEQILRGNVL------------------------FRPRLSKECCDLISR 234
                        330
                 ....*....|.
gi 119628251 311 MLAANPQDRPD 321
Cdd:cd14005  235 CLQFDPSKRPS 245
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
7-195 5.18e-14

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 70.95  E-value: 5.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKkirchapenVElalrefwalsSIKSQHPNVIHlEECILQKdgmvqkmsh 86
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK---------IE----------KKDSKHPQLEY-EAKVYKL--------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetsLKGEIAFdPRSAYYLW------FVMDFCdGGDMnEYLLSRKPNR---KTNTSFMLQLSSALAFLHK 157
Cdd:cd14016   52 --------------LQGGPGI-PRLYWFGQegdynvMVMDLL-GPSL-EDLFNKCGRKfslKTVLMLADQMISRLEYLHS 114
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119628251 158 NQIIHRDLKPDNILIsqtrlDTSDLEPTLKVADFGLSK 195
Cdd:cd14016  115 KGYIHRDIKPENFLM-----GLGKNSNKVYLIDFGLAK 147
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
12-319 5.26e-14

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 71.68  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIR---CHAPENVELALREFWALSsIKSQHPNVIHLEECIlqkdgmvQKMSHgs 88
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKkelVNDDEDIDWVQTEKHVFE-TASNHPFLVGLHSCF-------QTESR-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslylqlvetslkgeiafdprsayyLWFVMDFCDGGD-MNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd05588   71 --------------------------LFFVIEFVNGGDlMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrldtsDLEPTLKVADFGLSKvcsaSGQNPEEPVsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFALGII 246
Cdd:cd05588  125 DNVLL--------DSEGHIKLTDYGMCK----EGLRPGDTT-------STFCGTPNYIAPEILRGEdYGFSVDWWALGVL 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 247 IWAMLERITFIDTETKKEllgsYVKQGTEIVpVGEALLENPkmeLLIPvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd05588  186 MFEMLAGRSPFDIVGSSD----NPDQNTEDY-LFQVILEKP---IRIP---RSLSVKAASVLKGFLNKNPAER 247
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
115-251 6.06e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 71.53  E-value: 6.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05604   72 LYFVLDFVNGGELFFHLQRERSFPEPRARFYAaEIASALGYLHSINIVYRDLKPENILL--------DSQGHIVLTDFGL 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 194 SKvcsasgqnpeEPVSVNKCFLsTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05604  144 CK----------EGISNSDTTT-TFCGTPEYLAPEVIRKQpYDNTVDWWCLGSVLYEML 191
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
10-332 6.62e-14

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 70.91  E-value: 6.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRK---TSARVAVKKIR-CHAPENVELALREfwALSSIKSQHPNVIhleecilqkdgmvqkms 85
Cdd:cd05056   10 LGRCIGEGQFGDVYQGVYMSpenEKIAVAVKTCKnCTSPSVREKFLQE--AYIMRQFDHPHIV----------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetSLKGEIAFDPrsayyLWFVMDFCDGGDMNEYLLSRKPNRK--TNTSFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05056   71 --------------KLIGVITENP-----VWIVMELAPLGELRSYLQVNKYSLDlaSLILYAYQLSTALAYLESKRFVHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRldtsdlepTLKVADFGLSKVCSasgqnpEEPV---SVNKCFLStacgtdfYMAPE-VWEGHYTAKAD 239
Cdd:cd05056  132 DIAARNVLVSSPD--------CVKLGDFGLSRYME------DESYykaSKGKLPIK-------WMAPEsINFRRFTSASD 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 240 IFALGIIIWAMLERitfidteTKKELLGsyVKQGTEIVPV--GEALlenPKMELLIPvkkksmngRMKQLIKEMLAANPQ 317
Cdd:cd05056  191 VWMFGVCMWEILML-------GVKPFQG--VKNNDVIGRIenGERL---PMPPNCPP--------TLYSLMTKCWAYDPS 250
                        330
                 ....*....|....*
gi 119628251 318 DRPDAFELELRLVQI 332
Cdd:cd05056  251 KRPRFTELKAQLSDI 265
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
7-327 7.18e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 70.76  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK-----KIRCHAPENVELALREFWALSSIKSQHPNVIhleECILQKDGMV 81
Cdd:cd14199    3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKvlskkKLMRQAGFPRRPPPRGARAAPEGCTQPRGPI---ERVYQEIAIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMSHGSnsslYLQLVETslkgeiaFDPRSAYYLWFVMDFCDGGDMNEyLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQI 160
Cdd:cd14199   80 KKLDHPN----VVKLVEV-------LDDPSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQdLIKGIEYLHYQKI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnKCFLSTACGTDFYMAPEVW---EGHYTAK 237
Cdd:cd14199  148 IHRDVKPSNLLVGE--------DGHIKIADFGVSNEFEGS-----------DALLTNTVGTPAFMAPETLsetRKIFSGK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 238 A-DIFALGIIIWA--------MLERITFIDTETKKELLGsyvkqgteivpvgeallenpkmellIPvKKKSMNGRMKQLI 308
Cdd:cd14199  209 AlDVWAMGVTLYCfvfgqcpfMDERILSLHSKIKTQPLE-------------------------FP-DQPDISDDLKDLL 262
                        330
                 ....*....|....*....
gi 119628251 309 KEMLAANPQDRPDAFELEL 327
Cdd:cd14199  263 FRMLDKNPESRISVPEIKL 281
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
8-266 7.46e-14

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 70.39  E-value: 7.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrchapeNVELALREfwalssiksqhpNVIHleecilqKDGMVQKMSHg 87
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFV------NKKLMKRD------------QVTH-------ELGVLQSLQH- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsSLYLQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLS-RKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd14113   63 ---PQLVGLLDT-------FETPTSYIL--VLEMADQGRLLDYVVRwGNLTEEKIRFYLREILEALQYLHNCRIAHLDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQtrldtSDLEPTLKVADFGlskvcsasgqnpeEPVSVNKC-FLSTACGTDFYMAPEVWEGH-YTAKADIFALG 244
Cdd:cd14113  131 PENILVDQ-----SLSKPTIKLADFG-------------DAVQLNTTyYIHQLLGSPEFAAPEIILGNpVSLTSDLWSIG 192
                        250       260
                 ....*....|....*....|...
gi 119628251 245 IIIWAMLERIT-FIDTETKKELL 266
Cdd:cd14113  193 VLTYVLLSGVSpFLDESVEETCL 215
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
14-251 7.75e-14

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 71.06  E-value: 7.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEaVIRKTSARVavkkirchapenvelalrefWALSSIKSQHpnvihleecILQKdgmvQKMSHGSNSSLY 93
Cdd:cd05585    2 IGKGSFGKVMQ-VRKKDTSRI--------------------YALKTIRKAH---------IVSR----SEVTHTLAERTV 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNeYLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd05585   48 LAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGELF-HHLQREGRFDLSRArfYTAELLCALECLHKFNVIYRDLKPENIL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 IsqtrldtsDLEPTLKVADFGLSKVcsasgqNPEEPVSVNkcflsTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAM 250
Cdd:cd05585  127 L--------DYTGHIALCDFGLCKL------NMKDDDKTN-----TFCGTPEYLAPELLLGHgYTKAVDWWTLGVLLYEM 187

                 .
gi 119628251 251 L 251
Cdd:cd05585  188 L 188
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
14-320 7.84e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 70.60  E-value: 7.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSArVAVKKIRCHAPENVELAL-REFWALSSIKsqHPNVIHLEECIlqkdgmvqkMSHGSNSSL 92
Cdd:cd14664    1 IGRGGAGTVYKGVMPNGTL-VAVKRLKGEGTQGGDHGFqAEIQTLGMIR--HRNIVRLRGYC---------SNPTTNLLV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 YlqlvetslkgeiafdprsayylwfvmDFCDGGDMNEYLLSRKPNR-----KTNTSFMLQLSSALAFLHKN---QIIHRD 164
Cdd:cd14664   69 Y--------------------------EYMPNGSLGELLHSRPESQppldwETRQRIALGSARGLAYLHHDcspLIIHRD 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILisqtrLDtSDLEPtlKVADFGLSKVCSASGqnpeepvsvNKCFLSTAcGTDFYMAPE-VWEGHYTAKADIFAL 243
Cdd:cd14664  123 VKSNNIL-----LD-EEFEA--HVADFGLAKLMDDKD---------SHVMSSVA-GSYGYIAPEyAYTGKVSEKSDVYSY 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 244 GIIiwaMLERITfidteTKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGR--MKQLIKEML---AANPQD 318
Cdd:cd14664  185 GVV---LLELIT-----GKRPFDEAFLDDGVDIVDWVRGLLEEKKVEALVDPDLQGVYKLeeVEQVFQVALlctQSSPME 256

                 ..
gi 119628251 319 RP 320
Cdd:cd14664  257 RP 258
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
115-335 7.99e-14

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 71.27  E-value: 7.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMnEYLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFG 192
Cdd:cd05587   72 LYFVMEYVNGGDL-MYHIQQVGKFKEPVAvfYAAEIAVGLFFLHSKGIIYRDLKLDNVML--------DAEGHIKIADFG 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 193 LSKvcsasgQNPEEPVSVNkcflsTACGTDFYMAPEVWEGHYTAKA-DIFALGIIIWAMLERITFIDTETKKELLGSyvk 271
Cdd:cd05587  143 MCK------EGIFGGKTTR-----TFCGTPDYIAPEIIAYQPYGKSvDWWAYGVLLYEMLAGQPPFDGEDEDELFQS--- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 272 qgteivpVGEALLENPkmellipvkkKSMNGRMKQLIKEMLAANP--------------QDRP-----DAFELELRLVQI 332
Cdd:cd05587  209 -------IMEHNVSYP----------KSLSKEAVSICKGLLTKHPakrlgcgptgerdiKEHPffrriDWEKLERREIQP 271

                 ...
gi 119628251 333 AFK 335
Cdd:cd05587  272 PFK 274
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
12-248 8.41e-14

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 70.21  E-value: 8.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRchAPENV---ELALrEFWALSSIkSQHPNVIHLEecilqkdGMVQKMSHGS 88
Cdd:cd13975    6 RELGRGQYGVVYACDSWGGHFPCALKSVV--PPDDKhwnDLAL-EFHYTRSL-PKHERIVSLH-------GSVIDYSYGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLV--------ETSLKGEIAFDPRsayyLWFVMDFCDGgdmneyllsrkpnrktntsfmlqlssaLAFLHKNQI 160
Cdd:cd13975   75 GSSIAVLLImerlhrdlYTGIKAGLSLEER----LQIALDVVEG---------------------------IRFLHSQGL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnPEEPVSvnkcflSTACGTDFYMAPEVWEGHYTAKADI 240
Cdd:cd13975  124 VHRDIKLKNVLL--------DKKNRAKITDLGFCK--------PEAMMS------GSIVGTPIHMAPELFSGKYDNSVDV 181

                 ....*...
gi 119628251 241 FALGIIIW 248
Cdd:cd13975  182 YAFGILFW 189
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
8-250 9.52e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 9.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVE-LALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkmsH 86
Cdd:cd07873    4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPcTAIREVSLLKDLK--HANIVTLHDII-----------H 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNS-SLYLQLVETSLKgeiafdprsaYYLwfvmDFCdGGDMNEYllsrkpNRKTntsFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07873   71 TEKSlTLVFEYLDKDLK----------QYL----DDC-GNSINMH------NVKL---FLFQLLRGLAYCHRRKVLHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgTDFYMAPEVWEG--HYTAKADIFAL 243
Cdd:cd07873  127 KPQNLLINE--------RGELKLADFGLARAKSIPTKTYSNEVV-----------TLWYRPPDILLGstDYSTQIDMWGV 187

                 ....*..
gi 119628251 244 GIIIWAM 250
Cdd:cd07873  188 GCIFYEM 194
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
6-251 1.07e-13

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 69.94  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREVGRGSYGVVYEAV-------IRKTSARVAVKKI-RCHAPENVelaLREFWALSSIKSQHpNVIHLEECILQK 77
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEdklhdlyDRNKGRLVALKHIyPTSSPSRI---LNELECLERLGGSN-NVSGLITAFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  78 DGMVqkmshgsnsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLlsRKPNRKTNTSFMLQLSSALAFLHK 157
Cdd:cd14019   77 DQVV-----------------------------------AVLPYIEHDDFRDFY--RKMSLTDIRIYLRNLFKALKHVHS 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISqtrldtSDLEPTLKVaDFGLskvcsASGQNPEEPVSVNKcflstaCGTDFYMAPEVWE--GHYT 235
Cdd:cd14019  120 FGIIHRDVKPGNFLYN------RETGKGVLV-DFGL-----AQREEDRPEQRAPR------AGTRGFRAPEVLFkcPHQT 181
                        250
                 ....*....|....*.
gi 119628251 236 AKADIFALGIIIWAML 251
Cdd:cd14019  182 TAIDIWSAGVILLSIL 197
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
14-321 1.15e-13

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 69.73  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAvirKTSARVAVKKIRCHAPENVEL-ALR-EFWALSsiKSQHPNVIHLEECILQKD-GMVQKMSHGSns 90
Cdd:cd14062    1 IGSGSFGTVYKG---RWHGDVAVKKLNVTDPTPSQLqAFKnEVAVLR--KTRHVNILLFMGYMTKPQlAIVTQWCEGS-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLY--LQLVETslkgeiafdprsayylwfvmDFcdggDMNEYL-LSRkpnrktntsfmlQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd14062   74 SLYkhLHVLET--------------------KF----EMLQLIdIAR------------QTAQGMDYLHAKNIIHRDLKS 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISqtrldtSDLepTLKVADFGLSKVCS--ASGQNPEEPVsvnkcflstacGTDFYMAPEVW----EGHYTAKADIF 241
Cdd:cd14062  118 NNIFLH------EDL--TVKIGDFGLATVKTrwSGSQQFEQPT-----------GSILWMAPEVIrmqdENPYSFQSDVY 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 242 ALGIIIWAMLeritfidtetKKELLGSYVKQGTEIV-PVGEALLEnPKMELLIPVKKKSmngrMKQLIKEMLAANPQDRP 320
Cdd:cd14062  179 AFGIVLYELL----------TGQLPYSHINNRDQILfMVGRGYLR-PDLSKVRSDTPKA----LRRLMEDCIKFQRDERP 243

                 .
gi 119628251 321 D 321
Cdd:cd14062  244 L 244
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
14-248 1.23e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 70.33  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCH-APENVELALREFWALSSIKsqHPNVIHLEECILQKDGMVQKMSHgsnssl 92
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElSVKNKDRWCHEIQIMKKLN--HPNVVKACDVPEEMNFLVNDVPL------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEyLLSRKPN-----RKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd14039   73 ------------------------LAMEYCSGGDLRK-LLNKPENccglkESQVLSLLSDIGSGIQYLHENKIIHRDLKP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQTRLDTSDleptlKVADFGLSKvcsasgqnpeepvSVNKCFLSTA-CGTDFYMAPEVWEGH-YTAKADIFALGI 245
Cdd:cd14039  128 ENIVLQEINGKIVH-----KIIDLGYAK-------------DLDQGSLCTSfVGTLQYLAPELFENKsYTVTVDYWSFGT 189

                 ...
gi 119628251 246 IIW 248
Cdd:cd14039  190 MVF 192
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
5-324 1.32e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 70.67  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapeNV----ELALREFWALSSIKSQHPN----VIHLEECILQ 76
Cdd:cd14134   11 TNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR-----NVekyrEAAKIEIDVLETLAEKDPNgkshCVQLRDWFDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  77 KDGMVqkmshgsnsslylqlvetslkgeIAFDPrsayYLWFVMDFCDGGDMNEYllsrkpNRKTNTSFMLQLSSALAFLH 156
Cdd:cd14134   86 RGHMC-----------------------IVFEL----LGPSLYDFLKKNNYGPF------PLEHVQHIAKQLLEAVAFLH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTRLDTSDLE-----------PTLKVADFGlskvcSASGQNPEEPVSVNkcflstacgTDFYM 225
Cdd:cd14134  133 DLKLTHTDLKPENILLVDSDYVKVYNPkkkrqirvpksTDIKLIDFG-----SATFDDEYHSSIVS---------TRHYR 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 226 APEV-----WeghyTAKADIFALGIIIW------------------AMLERI--TFIDTETKKELLGS---YVKQGT--- 274
Cdd:cd14134  199 APEVilglgW----SYPCDVWSIGCILVelytgellfqthdnlehlAMMERIlgPLPKRMIRRAKKGAkyfYFYHGRldw 274
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119628251 275 -EIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd14134  275 pEGSSSGRSIKRVCKPLKRLMLLVDPEHRLLFDLIRKMLEYDPSKRITAKE 325
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
13-252 1.37e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 70.05  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDgmvqkmshgsnssl 92
Cdd:cd06657   27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDY--QHENVVEMYNSYLVGD-------------- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 ylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd06657   91 ---------------------ELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd06657  150 TH--------DGRVKLSDFGFCAQVSKEVPRRKSLV-----------GTPYWMAPElISRLPYGPEVDIWSLGIMVIEMV 210

                 .
gi 119628251 252 E 252
Cdd:cd06657  211 D 211
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
115-251 1.57e-13

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 70.42  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05598   76 LYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIaELVCAIESVHKMGFIHRDIKPDNILI--------DRDGHIKLTDFGL 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 194 skvCSAsgqnpeepvsvnkcFLST-------AC---GTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05598  148 ---CTG--------------FRWThdskyylAHslvGTPNYIAPEVLLRTgYTQLCDWWSVGVILYEML 199
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-250 1.66e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 70.06  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIrchapenvelalrEFWALSSIKSQhpnvihlEECILQKDgMVQKMSHGSNSS 91
Cdd:cd08229   30 KKIGRGQFSEVYRATCLLDGVPVALKKV-------------QIFDLMDAKAR-------ADCIKEID-LLKQLNHPNVIK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 LYLQLVETSlkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNR-----KTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd08229   89 YYASFIEDN-------------ELNIVLELADAGDLSRMIKHFKKQKrlipeKTVWKYFVQLCSALEHMHSRRVMHRDIK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEPVsvnkcflstacGTDFYMAPE-VWEGHYTAKADIFALGI 245
Cdd:cd08229  156 PANVFITATGV--------VKLGDLGLGRFFSSKTTAAHSLV-----------GTPYYMSPErIHENGYNFKSDIWSLGC 216

                 ....*
gi 119628251 246 IIWAM 250
Cdd:cd08229  217 LLYEM 221
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
13-251 1.73e-13

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 70.10  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIR--KTSARVAVKKIRCHAPENVelALREFWALSSIKsqHPNVIHLEECILqkdgmvqkmSHgSNS 90
Cdd:cd07867    9 KVGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGISMS--ACREIALLRELK--HPNVIALQKVFL---------SH-SDR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLqlvetslkgeiAFDpRSAYYLWFVMDFCDGGDMNeyllsRKP---NRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd07867   75 KVWL-----------LFD-YAEHDLWHIIKFHRASKAN-----KKPmqlPRSMVKSLLYQILDGIHYLHANWVLHRDLKP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrLDTSDLEPTLKVADFGLSKVCSAsgqnPEEPVSVnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFALGI 245
Cdd:cd07867  138 ANILV----MGEGPERGRVKIADMGFARLFNS----PLKPLAD----LDPVVVTFWYRAPELLLGarHYTKAIDIWAIGC 205

                 ....*.
gi 119628251 246 IIWAML 251
Cdd:cd07867  206 IFAELL 211
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
8-268 1.81e-13

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 69.60  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI---------RCHAPENVElalREFWALSSIksQHPNVIHLEECILQKD 78
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsrasrRGVSREEIE---REVSILRQV--LHPNIITLHDVYENRT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 GMVqkmshgsnssLYLQLVEtslkgeiafdprsayylwfvmdfcdGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHK 157
Cdd:cd14196   82 DVV----------LILELVS-------------------------GGELFDFLAQKESlSEEEATSFIKQILDGVNYLHT 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGLSkvcsasgQNPEEPVSVNKCFlstacGTDFYMAPEVWegHYTA- 236
Cdd:cd14196  127 KKIAHFDLKPENIML----LDKNIPIPHIKLIDFGLA-------HEIEDGVEFKNIF-----GTPEFVAPEIV--NYEPl 188
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119628251 237 --KADIFALGIIIWAMLERITFIDTETKKELLGS 268
Cdd:cd14196  189 glEADMWSIGVITYILLSGASPFLGDTKQETLAN 222
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
115-255 1.87e-13

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 69.60  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTN--TSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFG 192
Cdd:cd14221   65 LNFITEYIKGGTLRGIIKSMDSHYPWSqrVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENK--------SVVVADFG 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 193 LSKVCSASGQNPEEPVSVNKCFLS---TACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAMLERIT 255
Cdd:cd14221  137 LARLMVDEKTQPEGLRSLKKPDRKkryTVVGNPYWMAPEMINGRsYDEKVDVFSFGIVLCEIIGRVN 203
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
114-251 1.90e-13

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 70.03  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEyLLSRKPNR--KTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILISQTrldtsdlePTLKVAD 190
Cdd:cd05601   75 NLYLVMEYHPGGDLLS-LLSRYDDIfeESMARFYLaELVLAIHSLHSMGYVHRDIKPENILIDRT--------GHIKLAD 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 191 FGLSKVCSASGQ-NPEEPVsvnkcflstacGTDFYMAPEV-------WEGHYTAKADIFALGIIIWAML 251
Cdd:cd05601  146 FGSAAKLSSDKTvTSKMPV-----------GTPDYIAPEVltsmnggSKGTYGVECDWWSLGIVAYEML 203
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
7-317 1.95e-13

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 70.07  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALREFWALSSIKS-QHPNVIhleecilqkdGMVQKMS 85
Cdd:cd07877   18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLS-RPFQSIIHAKRTYRELRLLKHmKHENVI----------GLLDVFT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGsnsslylqlveTSLKgeiafDPRSAYYLWFVMdfcdGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07877   87 PA-----------RSLE-----EFNDVYLVTHLM----GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsDLEptLKVADFGLSKvcsasgQNPEEpvsvnkcfLSTACGTDFYMAPEV---WEgHYTAKADIFA 242
Cdd:cd07877  147 KPSNLAVNE------DCE--LKILDFGLAR------HTDDE--------MTGYVATRWYRAPEImlnWM-HYNQTVDIWS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 243 LGIIIWAMLE-RITFIDTEtkkellgsYVKQGTEIVpvgeALLENPKMELLIPVKKKSMNGRMKQLIKE--------MLA 313
Cdd:cd07877  204 VGCIMAELLTgRTLFPGTD--------HIDQLKLIL----RLVGTPGAELLKKISSESARNYIQSLTQMpkmnfanvFIG 271

                 ....
gi 119628251 314 ANPQ 317
Cdd:cd07877  272 ANPL 275
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
11-325 1.96e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 69.67  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL--ALREFWAlSSIKSQHPNVIHLEECILQKDGMVQKMSHGS 88
Cdd:cd14138   10 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEqnALREVYA-HAVLGQHSHVVRYYSAWAEDDHMLIQNEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLylqlvetslKGEIAFDPRSAYYLwfvmdfcdggdmneyllsRKPNRKtntSFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd14138   89 GGSL---------ADAISENYRIMSYF------------------TEPELK---DLLLQVARGLKYIHSMSLVHMDIKPS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTRLDTSDLEP-----------TLKVADFGlsKVCSASGQNPEEpvsvnkcflstacGTDFYMAPEVWEGHYT-- 235
Cdd:cd14138  139 NIFISRTSIPNAASEEgdedewasnkvIFKIGDLG--HVTRVSSPQVEE-------------GDSRFLANEVLQENYThl 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 236 AKADIFALGIIIWAmleritfidtetkkellgsyvKQGTEIVPV-GEALLENPKMELliPVKKKSMNGRMKQLIKEMLAA 314
Cdd:cd14138  204 PKADIFALALTVVC---------------------AAGAEPLPTnGDQWHEIRQGKL--PRIPQVLSQEFLDLLKVMIHP 260
                        330
                 ....*....|.
gi 119628251 315 NPQDRPDAFEL 325
Cdd:cd14138  261 DPERRPSAVAL 271
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
7-268 2.01e-13

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 70.14  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIR------CHAPEnvelALREFWALSSIKsqHPNVIHLEECILQKdgm 80
Cdd:cd07850    1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpfqnvTHAKR----AYRELVLMKLVN--HKNIIGLLNVFTPQ--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  81 vQKMSHGSNSSLYLQLVETSLKGEIAFD---PRSAYYLWfvmdfcdggdmneyllsrkpnrktntsfmlQLSSALAFLHK 157
Cdd:cd07850   72 -KSLEEFQDVYLVMELMDANLCQVIQMDldhERMSYLLY------------------------------QMLCGIKHLHS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISqtrldtSDLepTLKVADFGLSKvcSASGQNPEEPVSVnkcflstacgTDFYMAPEVWEGH-YTA 236
Cdd:cd07850  121 AGIIHRDLKPSNIVVK------SDC--TLKILDFGLAR--TAGTSFMMTPYVV----------TRYYRAPEVILGMgYKE 180
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 119628251 237 KADIFALGIIIWAML-ERITF-----IDTETK-KELLGS 268
Cdd:cd07850  181 NVDIWSVGCIMGEMIrGTVLFpgtdhIDQWNKiIEQLGT 219
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
11-245 2.02e-13

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 69.31  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENvelalrefwalsSIKSQHPNVIHLEECilqkdgmvqkmshgsNS 90
Cdd:cd06640    9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED------------EIEDIQQEITVLSQC---------------DS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLQLVETSLKGEiafdprsayYLWFVMDFCDGGDMNEyLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd06640   62 PYVTKYYGSYLKGT---------KLWIIMEYLGGGSALD-LLRAGPFDEFQIATMLkEILKGLDYLHSEKKIHRDIKAAN 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 170 ILISQtrldtsdlEPTLKVADFGLskvcsaSGQNPEEPVSVNkcflsTACGTDFYMAPEV-WEGHYTAKADIFALGI 245
Cdd:cd06640  132 VLLSE--------QGDVKLADFGV------AGQLTDTQIKRN-----TFVGTPFWMAPEViQQSAYDSKADIWSLGI 189
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
7-252 2.05e-13

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 70.08  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALREFWALSSIKS-QHPNVIHLeecilqkdgmvqkms 85
Cdd:cd07878   16 RYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS-RPFQSLIHARRTYRELRLLKHmKHENVIGL--------------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslyLQLVETSLKGEiafDPRSAYYLWFVMdfcdGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07878   80 --------LDVFTPATSIE---NFNEVYLVTNLM----GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsDLEptLKVADFGLSKvcsasgQNPEEpvsvnkcfLSTACGTDFYMAPEV---WEgHYTAKADIFA 242
Cdd:cd07878  145 KPSNVAVNE------DCE--LRILDFGLAR------QADDE--------MTGYVATRWYRAPEImlnWM-HYNQTVDIWS 201
                        250
                 ....*....|
gi 119628251 243 LGIIIWAMLE 252
Cdd:cd07878  202 VGCIMAELLK 211
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
119-325 2.09e-13

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 69.23  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNEYLLSRKPNRKTNT---SFMLQLSSALAFLHKNQ--IIHRDLKPDNILISQTRLdtsdleptLKVADFGL 193
Cdd:cd14037   85 MEYCKGGGVIDLMNQRLQTGLTESeilKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGN--------YKLCDFGS 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 SKVCSASGQNP------EEPVSVNkcflSTACgtdfYMAPEVWEGH----YTAKADIFALGIiiwaMLERITFIDTetkk 263
Cdd:cd14037  157 ATTKILPPQTKqgvtyvEEDIKKY----TTLQ----YRAPEMIDLYrgkpITEKSDIWALGC----LLYKLCFYTT---- 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 264 ellgsyvkqgteivPVGE----ALLeNPKMEllIPVKKKSMNgRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14037  221 --------------PFEEsgqlAIL-NGNFT--FPDNSRYSK-RLHKLIRYMLEEDPEKRPNIYQV 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
74-263 2.33e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 70.11  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDGMVQK--MSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-LQLSS 150
Cdd:cd05593   47 ILKKEVIIAKdeVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYgAEIVS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSvNKCFLSTACGTDFYMAPEVW 230
Cdd:cd05593  127 ALDYLHSGKIVYRDLKLENLML--------DKDGHIKITDFGLCK----------EGIT-DAATMKTFCGTPEYLAPEVL 187
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119628251 231 EGH-YTAKADIFALGIIIWAML-ERITFIDTETKK 263
Cdd:cd05593  188 EDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHEK 222
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
7-250 2.83e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 68.88  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLirEVGRGSYGVVYEAVIRKTSARVA---------VKKIRCHAPENVELalrefwaLSSIksQHPNVIHleecilqk 77
Cdd:cd14033    4 KFNI--EIGRGSFKTVYRGLDTETTVEVAwcelqtrklSKGERQRFSEEVEM-------LKGL--QHPNIVR-------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  78 dgmvqkmshgsnsslYLQLVETSLKGEIAfdprsayyLWFVMDFCDGGDMNEYLLS-RKPNRKTNTSFMLQLSSALAFLH 156
Cdd:cd14033   65 ---------------FYDSWKSTVRGHKC--------IILVTELMTSGTLKTYLKRfREMKLKLLQRWSRQILKGLHFLH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQ--IIHRDLKPDNILISQtrldtsdlePT--LKVADFGLSKVCSASgqnpeepvsvnkcFLSTACGTDFYMAPEVWEG 232
Cdd:cd14033  122 SRCppILHRDLKCDNIFITG---------PTgsVKIGDLGLATLKRAS-------------FAKSVIGTPEFMAPEMYEE 179
                        250
                 ....*....|....*...
gi 119628251 233 HYTAKADIFALGIIIWAM 250
Cdd:cd14033  180 KYDEAVDVYAFGMCILEM 197
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
115-251 3.13e-13

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 69.36  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05584   75 LYLILEYLSGGELFMHLEREGIFMEDTACFYLaEITLALGHLHSLGIIYRDLKPENILL--------DAQGHVKLTDFGL 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 skvCSASGQNPEepvsvnkcFLSTACGTDFYMAPEVW--EGHYTAkADIFALGIIIWAML 251
Cdd:cd05584  147 ---CKESIHDGT--------VTHTFCGTIEYMAPEILtrSGHGKA-VDWWSLGALMYDML 194
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
96-250 3.19e-13

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 69.52  E-value: 3.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  96 LVETSLKGE-----IAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd05586   47 LVRTALDESpfivgLKFSFQTPTDLYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIaELVLALEHLHKNDIVYRDLKPEN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeePVSVNKCFLSTACGTDFYMAPEVW--EGHYTAKADIFALGIII 247
Cdd:cd05586  127 ILL--------DANGHIALCDFGLSK-----------ADLTDNKTTNTFCGTTEYLAPEVLldEKGYTKMVDFWSLGVLV 187

                 ...
gi 119628251 248 WAM 250
Cdd:cd05586  188 FEM 190
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
14-253 4.25e-13

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 68.93  E-value: 4.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTsaRVAVKkirCHAPENVE--LALREFWALSSIksQHPNVIHleeCILQKDGMVQkmshgsnss 91
Cdd:cd14054    3 IGQGRYGTVWKGSLDER--PVAVK---VFPARHRQnfQNEKDIYELPLM--EHSNILR---FIGADERPTA--------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH---------KNQIIH 162
Cdd:cd14054   64 ----------------DGRMEYLL--VLEYAPKGSLCSYLRENTLDWMSSCRMALSLTRGLAYLHtdlrrgdqyKPAIAH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISqtrldtSDLepTLKVADFGLS-KVCSASGQNPEEPVSVNKCFlsTACGTDFYMAPEVWEG--------H 233
Cdd:cd14054  126 RDLNSRNVLVK------ADG--SCVICDFGLAmVLRGSSLVRGRPGAAENASI--SEVGTLRYMAPEVLEGavnlrdceS 195
                        250       260
                 ....*....|....*....|
gi 119628251 234 YTAKADIFALGIIIWAMLER 253
Cdd:cd14054  196 ALKQVDVYALGLVLWEIAMR 215
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
10-248 4.49e-13

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 68.08  E-value: 4.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKTsaRVAVKKIRCHApenvelALREFWALSSIKSQ--HPNVIHLEECILQKDGmvqkmshg 87
Cdd:cd05082   10 LLQTIGKGEFGDVMLGDYRGN--KVAVKCIKNDA------TAQAFLAEASVMTQlrHSNLVQLLGVIVEEKG-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPN---RKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd05082   74 ---GLYI-----------------------VTEYMAKGSLVDYLRSRGRSvlgGDCLLKFSLDVCEAMEYLEGNNFVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVSvnkcflstacgtdfYMAPEVW-EGHYTAKADIFAL 243
Cdd:cd05082  128 LAARNVLVSE--------DNVAKVSDFGLTKEASSTQDTGKLPVK--------------WTAPEALrEKKFSTKSDVWSF 185

                 ....*
gi 119628251 244 GIIIW 248
Cdd:cd05082  186 GILLW 190
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
13-251 5.41e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 68.93  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIR--KTSARVAVKKIRCHAPENVelALREFWALSSIKsqHPNVIHLEECILqkdgmvqkmSHGSNS 90
Cdd:cd07868   24 KVGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGISMS--ACREIALLRELK--HPNVISLQKVFL---------SHADRK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLqlvetslkgeiaFDpRSAYYLWFVMDFCDGGDMNeyllsRKP---NRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd07868   91 VWLL------------FD-YAEHDLWHIIKFHRASKAN-----KKPvqlPRGMVKSLLYQILDGIHYLHANWVLHRDLKP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrLDTSDLEPTLKVADFGLSKVCSAsgqnPEEPVSVnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFALGI 245
Cdd:cd07868  153 ANILV----MGEGPERGRVKIADMGFARLFNS----PLKPLAD----LDPVVVTFWYRAPELLLGarHYTKAIDIWAIGC 220

                 ....*.
gi 119628251 246 IIWAML 251
Cdd:cd07868  221 IFAELL 226
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
14-335 5.45e-13

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 68.22  E-value: 5.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVEL--ALREFWALSSiKSQHPNVIHLEecilqkdGMVQKMSHgs 88
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVsfcRNSSSEQEEVveAIREEIRMMA-RLNHPNIVRML-------GATQHKSH-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslYLQLVETSLKGEIAfdprsayylwfvmdfcdggdmneYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd06630   78 ----FNIFVEWMAGGSVA-----------------------SLLSKYGAFSENViiNYTLQILRGLAYLHDNQIIHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRLDtsdleptLKVADFGLSKVCSASGQNPEEpvsvnkcFLSTACGTDFYMAPEVWEG-HYTAKADIFALGI 245
Cdd:cd06630  131 GANLLVDSTGQR-------LRIADFGAAARLASKGTGAGE-------FQGQLLGTIAFMAPEVLRGeQYGRSCDVWSVGC 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 246 IIWAMLERITFIDTETKKELLGSYVKQGTEIVPvgeallenpkmelliPVKKKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd06630  197 VIIEMATAKPPWNAEKISNHLALIFKIASATTP---------------PPIPEHLSPGLRDVTLRCLELQPEDRPPAREL 261
                        330
                 ....*....|
gi 119628251 326 elrLVQIAFK 335
Cdd:cd06630  262 ---LKHPVFT 268
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
3-194 8.16e-13

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 67.95  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   3 SSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchaPENVELALREFWALSSIKSqHPNVIHLEEcilqkdgmvq 82
Cdd:cd14132   15 GSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLK---PVKKKKIKREIKILQNLRG-GPNIVKLLD---------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetslkgeIAFDPRSAYYLwFVMDFCDGGDMNE--YLLSRKPNRktntSFMLQLSSALAFLHKNQI 160
Cdd:cd14132   81 ----------------------VVKDPQSKTPS-LIFEYVNNTDFKTlyPTLTDYDIR----YYMYELLKALDYCHSKGI 133
                        170       180       190
                 ....*....|....*....|....*....|....
gi 119628251 161 IHRDLKPDNILISQTRldtsdlePTLKVADFGLS 194
Cdd:cd14132  134 MHRDVKPHNIMIDHEK-------RKLRLIDWGLA 160
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
8-251 8.44e-13

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 68.52  E-value: 8.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapENVELALREFwalssiksqhpNVIHLEECILQKDgmvqkmshg 87
Cdd:cd05600   13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMK----KKVLFKLNEV-----------NHVLTERDILTTT--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 sNSSLYLQLVetslkgeIAFDPRSayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd05600   69 -NSPWLVKLL-------YAFQDPE--NVYLAMEYVPGGDFRTLLNNSGILSEEHARFyIAEMFAAISSLHQLGYIHRDLK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSK------VCSASGQNPEEPVSVNKCFLS--------------------TACG 220
Cdd:cd05600  139 PENFLI--------DSSGHIKLTDFGLASgtlspkKIESMKIRLEEVKNTAFLELTakerrniyramrkedqnyanSVVG 210
                        250       260       270
                 ....*....|....*....|....*....|..
gi 119628251 221 TDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd05600  211 SPDYMAPEVLRGEgYDLTVDYWSLGCILFECL 242
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
53-251 9.04e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 68.31  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  53 EFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHgsnsslylQLVETSLKGEIafDPRSAYylwFVMDFCDGGDMNEYLl 132
Cdd:PTZ00263  44 EYYAIKCLKKREILKMKQVQHVAQEKSILMELSH--------PFIVNMMCSFQ--DENRVY---FLLEFVVGGELFTHL- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 133 sRKPNRKTNTS---FMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgQNPEEPVs 209
Cdd:PTZ00263 110 -RKAGRFPNDVakfYHAELVLAFEYLHSKDIIYRDLKPENLLL--------DNKGHVKVTDFGFAK------KVPDRTF- 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119628251 210 vnkcflsTACGTDFYMAPEVWE--GHYTAkADIFALGIIIWAML 251
Cdd:PTZ00263 174 -------TLCGTPEYLAPEVIQskGHGKA-VDWWTMGVLLYEFI 209
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-264 1.04e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 67.27  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLI--REVGRGSYGVVYEAVIRKTSARVAVKKIR-------CHAPENVELALREFWALSsiksqhPNVIHLEECIL 75
Cdd:cd14197    6 QERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRkrrkgqdCRMEIIHEIAVLELAQAN------PWVINLHEVYE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  76 QKDGMVQKMSHGSNSSLYLQLVetslkgeiafdprsayylwfvmdfcdgGDMNEYLLSRKPNRktntsFMLQLSSALAFL 155
Cdd:cd14197   80 TASEMILVLEYAAGGEIFNQCV---------------------------ADREEAFKEKDVKR-----LMKQILEGVSFL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILIsqtrldTSDlEP--TLKVADFGLSKVCSasgqNPEEpvsvnkcfLSTACGTDFYMAPEV--WE 231
Cdd:cd14197  128 HNNNVVHLDLKPQNILL------TSE-SPlgDIKIVDFGLSRILK----NSEE--------LREIMGTPEYVAPEIlsYE 188
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119628251 232 GHYTAkADIFALGIIIWAMLERITFIDTETKKE 264
Cdd:cd14197  189 PISTA-TDMWSIGVLAYVMLTGISPFLGDDKQE 220
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
10-248 1.11e-12

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 67.41  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIR-----KTSARVAVKKIRCHAPENVELA-LREfwALSSIKSQHPNVIHleeCIlqkdgmvqk 83
Cdd:cd05036   10 LIRALGQGAFGEVYEGTVSgmpgdPSPLQVAVKTLPELCSEQDEMDfLME--ALIMSKFNHPNIVR---CI--------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshgsnsslylqlvetslkgEIAFDpRSAYYLwfVMDFCDGGDMNEYL-LSRKPNRKTNTSFM---LQLSSALA----FL 155
Cdd:cd05036   76 --------------------GVCFQ-RLPRFI--LLELMAGGDLKSFLrENRPRPEQPSSLTMldlLQLAQDVAkgcrYL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILisqtrLDTSDLEPTLKVADFGLSK-VCSAS----GQNPEEPVSvnkcflstacgtdfYMAPEVW 230
Cdd:cd05036  133 EENHFIHRDIAARNCL-----LTCKGPGRVAKIGDFGMARdIYRADyyrkGGKAMLPVK--------------WMPPEAF 193
                        250
                 ....*....|....*....
gi 119628251 231 -EGHYTAKADIFALGIIIW 248
Cdd:cd05036  194 lDGIFTSKTDVWSFGVLLW 212
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
8-254 1.19e-12

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 67.41  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVEL-ALREFWALSSIKsqHPNVIHLEECILQKDGMvqkmsh 86
Cdd:cd07869    7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFtAIREASLLKGLK--HANIVLLHDIIHTKETL------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsSLYLQLVETSLkgeiafdprSAYylwfvMDFCDGGdmneyllSRKPNRKTntsFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd07869   79 ----TLVFEYVHTDL---------CQY-----MDKHPGG-------LHPENVKL---FLFQLLRGLSYIHQRYILHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISqtrlDTSDleptLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFALG 244
Cdd:cd07869  131 PQNLLIS----DTGE----LKLADFGLARAKSVPSHT-----------YSNEVVTLWYRPPDVLLGstEYSTCLDMWGVG 191
                        250
                 ....*....|
gi 119628251 245 IIIWAMLERI 254
Cdd:cd07869  192 CIFVEMIQGV 201
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-322 1.21e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 67.25  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIR-------CHAPenvelALREFWALSSIKSqHPNVIHLEEcilqkdgmvqkm 84
Cdd:cd14198   14 KELGRGKFAVVRQCISKSTGQEYAAKFLKkrrrgqdCRAE-----ILHEIAVLELAKS-NPRVVNLHE------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqLVETslkgeiafdprsAYYLWFVMDFCDGGDMNEYLLSRKPNRKTN---TSFMLQLSSALAFLHKNQII 161
Cdd:cd14198   76 -----------VYET------------TSEIILILEYAAGGEIFNLCVPDLAEMVSEndiIRLIRQILEGVYYLHQNNIV 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdLEP--TLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWegHY---TA 236
Cdd:cd14198  133 HLDLKPQNILLSS-------IYPlgDIKIVDFGMSRKIGHACE------------LREIMGTPEYLAPEIL--NYdpiTT 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMLERITFIDTETKKEllgSYVKQGTEIVPVGEALLEnpkmellipvkkkSMNGRMKQLIKEMLAANP 316
Cdd:cd14198  192 ATDMWNIGVIAYMLLTHESPFVGEDNQE---TFLNISQVNVDYSEETFS-------------SVSQLATDFIQKLLVKNP 255

                 ....*.
gi 119628251 317 QDRPDA 322
Cdd:cd14198  256 EKRPTA 261
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
11-325 1.39e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 66.87  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPE--NVELALREFWAlSSIKSQHPNVIHLEECILQKDGMVQKMSHGS 88
Cdd:cd14139    5 LEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGssNEQLALHEVYA-HAVLGHHPHVVRYYSAWAEDDHMIIQNEYCN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETSLKGEiafdprsayylwfvmdFCDGGDMNEYLlsrkpnrktntsfmLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd14139   84 GGSLQDAISENTKSGN----------------HFEEPELKDIL--------------LQVSMGLKYIHNSGLVHLDIKPS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILI--------------SQTRLDTSDLEPTLKVADFGlsKVCSASGQNPEEpvsvnkcflstacGTDFYMAPEVWEGHY 234
Cdd:cd14139  134 NIFIchkmqsssgvgeevSNEEDEFLSANVVYKIGDLG--HVTSINKPQVEE-------------GDSRFLANEILQEDY 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 T--AKADIFALGIIIwamleritfidtetkkellgsYVKQGTEIVPVGEALLENPKMELLIPVKKKsMNGRMKQLIKEML 312
Cdd:cd14139  199 RhlPKADIFALGLTV---------------------ALAAGAEPLPTNGAAWHHIRKGNFPDVPQE-LPESFSSLLKNMI 256
                        330
                 ....*....|...
gi 119628251 313 AANPQDRPDAFEL 325
Cdd:cd14139  257 QPDPEQRPSATAL 269
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
14-290 1.51e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 67.02  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSAR----VAVKKIRCH--APENVElalREFWALSSIKsqHPNVihleecilqkdgmvqkmshg 87
Cdd:cd14055    3 VGKGRFAEVWKAKLKQNASGqyetVAVKIFPYEeyASWKNE---KDIFTDASLK--HENI-------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslyLQLVETSLKGEiafDPRSAYylWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH---------KN 158
Cdd:cd14055   58 ------LQFLTAEERGV---GLDRQY--WLITAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHsdrtpcgrpKI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISqtrldtSDLEPTLkvADFGLSKVCSASgqnpeepVSVNKCFLSTACGTDFYMAPEVWEGHYT--- 235
Cdd:cd14055  127 PIAHRDLKSSNILVK------NDGTCVL--ADFGLALRLDPS-------LSVDELANSGQVGTARYMAPEALESRVNled 191
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 236 ----AKADIFALGIIIWAMLERITFIDTETKKELlgsyvkqgteivPVGEALLENPKME 290
Cdd:cd14055  192 lesfKQIDVYSMALVLWEMASRCEASGEVKPYEL------------PFGSKVRERPCVE 238
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-251 1.56e-12

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 67.64  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYeaVIRKTSARVAVKkirchapenvelalrefwaLSSIKsqhpnvihleecILQKDGMVQK---M 84
Cdd:cd05614    2 FELLKVLGTGAYGKVF--LVRKVSGHDANK-------------------LYAMK------------VLRKAALVQKaktV 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLQLVETS---LKGEIAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQI 160
Cdd:cd05614   49 EHTRTERNVLEHVRQSpflVTLHYAFQTDAKLHL--ILDYVSGGELFTHLYQRDHFSEDEVRFYSgEIILALEHLHKLGI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKvcsasgqnpeEPVSVNKCFLSTACGTDFYMAPEVWE---GHYTAk 237
Cdd:cd05614  127 VYRDIKLENILL--------DSEGHVVLTDFGLSK----------EFLTEEKERTYSFCGTIEYMAPEIIRgksGHGKA- 187
                        250
                 ....*....|....
gi 119628251 238 ADIFALGIIIWAML 251
Cdd:cd05614  188 VDWWSLGILMFELL 201
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-251 1.60e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 66.99  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 111 SAYYLWFVMDFCDGGDMNEYLLSRK-PNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISqtrldTSDLEPTLKVA 189
Cdd:cd14168   79 SPNHLYLVMQLVSGGELFDRIVEKGfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYF-----SQDEESKIMIS 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 190 DFGLSKVcSASGQnpeepvsvnkcFLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAML 251
Cdd:cd14168  154 DFGLSKM-EGKGD-----------VMSTACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILL 204
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
115-251 1.76e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 67.73  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRK--PNRKTNTsFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFG 192
Cdd:cd05626   76 LYFVMDYIPGGDMMSLLIRMEvfPEVLARF-YIAELTLAIESVHKMGFIHRDIKPDNILI--------DLDGHIKLTDFG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 193 L---------SKVCSASG---QNPEEPVSV------------------------NKCFLSTACGTDFYMAPEV-WEGHYT 235
Cdd:cd05626  147 LctgfrwthnSKYYQKGShirQDSMEPSDLwddvsncrcgdrlktleqratkqhQRCLAHSLVGTPNYIAPEVlLRKGYT 226
                        170
                 ....*....|....*.
gi 119628251 236 AKADIFALGIIIWAML 251
Cdd:cd05626  227 QLCDWWSVGVILFEML 242
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
14-325 1.91e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 66.19  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCH--APENVELALRefwalssikSQHPNVIHLEECILQKDGMVQKMSHGsnss 91
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEqfKPSDVEIQAC---------FRHENIAELYGALLWEETVHLFMEAG---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylqlvetslkgeiafdprsayylwfvmdfcDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd13995   79 -------------------------------EGGSVLEKLESCGPMREFEIIWVTKhVLKGLDFLHSKNIIHHDIKPSNI 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LISQTRldtsdleptLKVADFGLSKVCSASGQNPEEpvsvnkcflstACGTDFYMAPEV--WEGHYTaKADIFALGIIIW 248
Cdd:cd13995  128 VFMSTK---------AVLVDFGLSVQMTEDVYVPKD-----------LRGTEIYMSPEVilCRGHNT-KADIYSLGATII 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 249 AMLERITFIDTETKKELLGSYV----KQGteivpvgeallenPKMELLipvkKKSMNGRMKQLIKEMLAANPQDRPDAFE 324
Cdd:cd13995  187 HMQTGSPPWVRRYPRSAYPSYLyiihKQA-------------PPLEDI----AQDCSPAMRELLEAALERNPNHRSSAAE 249

                 .
gi 119628251 325 L 325
Cdd:cd13995  250 L 250
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
14-264 2.09e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 66.40  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVELALREFWALSSIKSqhPNVIHLEecilqkdgmvqkmshgsns 90
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLdkkRIKKKKGETMALNEKIILEKVSS--PFIVSLA------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylqlvetslkgeIAFDPRSAyyLWFVMDFCDGGDMnEYLLSRKPNRKTNTSFML----QLSSALAFLHKNQIIHRDLK 166
Cdd:cd05577   60 --------------YAFETKDK--LCLVLTLMNGGDL-KYHIYNVGTRGFSEARAIfyaaEIICGLEHLHNRFIVYRDLK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSkvCSASGQNPeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFALG 244
Cdd:cd05577  123 PENILL--------DDHGHVRISDLGLA--VEFKGGKK----------IKGRVGTHGYMAPEVLQKevAYDFSVDWFALG 182
                        250       260
                 ....*....|....*....|.
gi 119628251 245 IIIWAMLE-RITFIDTETKKE 264
Cdd:cd05577  183 CMLYEMIAgRSPFRQRKEKVD 203
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
115-319 2.19e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 66.60  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDmneyLLSRKPNR-------KTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTsdlepTLK 187
Cdd:cd14170   74 LLIVMECLDGGE----LFSRIQDRgdqafteREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNA-----ILK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 188 VADFGLSKvcsasgqnpeEPVSVNKcfLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWAMLERITFIdtetkkell 266
Cdd:cd14170  145 LTDFGFAK----------ETTSHNS--LTTPCYTPYYVAPEVLgPEKYDKSCDMWSLGVIMYILLCGYPPF--------- 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119628251 267 gsYVKQGTEIVPVGEALLENPKMELLIPvKKKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14170  204 --YSNHGLAISPGMKTRIRMGQYEFPNP-EWSEVSEEVKMLIRNLLKTEPTQR 253
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
11-245 2.29e-12

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 66.23  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENvelalrefwalsSIKSQHPNVIHLEECilqkdgmvqkmshgsNS 90
Cdd:cd06642    9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED------------EIEDIQQEITVLSQC---------------DS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLQLVETSLKGEiafdprsayYLWFVMDFCDGGDMNEyLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd06642   62 PYITRYYGSYLKGT---------KLWIIMEYLGGGSALD-LLKPGPLEETYIATILrEILKGLDYLHSERKIHRDIKAAN 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 170 ILISQtrldtsdlEPTLKVADFGLskvcsaSGQNPEEPVSVNkcflsTACGTDFYMAPEVW-EGHYTAKADIFALGI 245
Cdd:cd06642  132 VLLSE--------QGDVKLADFGV------AGQLTDTQIKRN-----TFVGTPFWMAPEVIkQSAYDFKADIWSLGI 189
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
106-251 2.30e-12

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 66.26  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 106 AFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEP 184
Cdd:cd05583   67 AFQTDAKLHL--ILDYVNGGELFTHLYQREHFTESEVRIYIgEIVLALEHLHKLGIIYRDIKLENILL--------DSEG 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 185 TLKVADFGLSKvcsasgqnpeEPVSVNKCFLSTACGTDFYMAPEVW----EGHYTAkADIFALGIIIWAML 251
Cdd:cd05583  137 HVVLTDFGLSK----------EFLPGENDRAYSFCGTIEYMAPEVVrggsDGHDKA-VDWWSLGVLTYELL 196
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
14-248 2.32e-12

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 66.29  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELALREFWALSSIKsqHPNvihleecilqkdgMVQkmshgsnssly 93
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLK-EDTMEVEEFLKEAAVMKEIK--HPN-------------LVQ----------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetsLKGEIAFDPrsAYYLwfVMDFCDGGDMNEYLlsRKPNRKTNTSFML-----QLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd05052   67 -------LLGVCTREP--PFYI--ITEFMPYGNLLDYL--RECNREELNAVVLlymatQIASAMEYLEKKNFIHRDLAAR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTRLdtsdleptLKVADFGLSKVCSASgqnpeepvsvnkcfLSTA-CGTDF---YMAPE-VWEGHYTAKADIFAL 243
Cdd:cd05052  134 NCLVGENHL--------VKVADFGLSRLMTGD--------------TYTAhAGAKFpikWTAPEsLAYNKFSIKSDVWAF 191

                 ....*
gi 119628251 244 GIIIW 248
Cdd:cd05052  192 GVLLW 196
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
71-255 2.34e-12

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 66.00  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  71 EECILQKDGMVQKMSHgSNSSLYLQLVETSLKgeiafdprsayyLWFVMDFCDGGDMNEyLLSRKP---NRKTNTSFMLQ 147
Cdd:cd14156   32 QHKIVREISLLQKLSH-PNIVRYLGICVKDEK------------LHPILEYVSGGCLEE-LLAREElplSWREKVELACD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 148 LSSALAFLHKNQIIHRDLKPDNILISQTrldTSDLEPTlkVADFGLSK-VCSASGQNPEEPVSVnkcflstaCGTDFYMA 226
Cdd:cd14156   98 ISRGMVYLHSKNIYHRDLNSKNCLIRVT---PRGREAV--VTDFGLAReVGEMPANDPERKLSL--------VGSAFWMA 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 119628251 227 PEVWEGH-YTAKADIFALGIIIWAMLERIT 255
Cdd:cd14156  165 PEMLRGEpYDRKVDVFSFGIVLCEILARIP 194
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
4-248 3.57e-12

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 66.15  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   4 SQPKYDLIREVGRGSYGVVYEAVIR-----KTSARVAVKKIrchapeNVELALREfwalssiksqhpNVIHLEECILQKd 78
Cdd:cd05061    4 SREKITLLRELGQGSFGMVYEGNARdiikgEAETRVAVKTV------NESASLRE------------RIEFLNEASVMK- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkmshGSNSSLYLQLVETSLKGEIAFdprsayylwFVMDFCDGGDMNEYLLSRKPNRKTNTSF-------MLQLSS- 150
Cdd:cd05061   65 --------GFTCHHVVRLLGVVSKGQPTL---------VVMELMAHGDLKSYLRSLRPEAENNPGRppptlqeMIQMAAe 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ---ALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSAS-----GQNPEEPVSvnkcflstacgtd 222
Cdd:cd05061  128 iadGMAYLNAKKFVHRDLAARNCMVAH--------DFTVKIGDFGMTRDIYETdyyrkGGKGLLPVR------------- 186
                        250       260
                 ....*....|....*....|....*..
gi 119628251 223 fYMAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05061  187 -WMAPEsLKDGVFTTSSDMWSFGVVLW 212
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
11-320 4.03e-12

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 65.71  E-value: 4.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPenveLALREfwalssiksqhpnvihlEECILQKdgmvQKMSHGSNS 90
Cdd:cd14026    2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSP----VGDSE-----------------RNCLLKE----AEILHKARF 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLQLVEtslkgeIAFDPRsayYLWFVMDFCDGGDMNEyLLSRK---PNRKTNTSFMLQLSSALA--FLHKNQ--IIHR 163
Cdd:cd14026   57 SYILPILG------ICNEPE---FLGIVTEYMTNGSLNE-LLHEKdiyPDVAWPLRLRILYEIALGvnYLHNMSppLLHH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILIsqtrldtsDLEPTLKVADFGLSK--VCSASGQNPEEPVSVNkcflstacGTDFYMAPEVWEGHYTAKA--- 238
Cdd:cd14026  127 DLKTQNILL--------DGEFHVKIADFGLSKwrQLSISQSRSSKSAPEG--------GTIIYMPPEEYEPSQKRRAsvk 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 -DIFALGIIIWAMLER-ITFIDTETKKELLGSyVKQGTEIVPVGEAL-LENPKMELLIpvkkksmngrmkQLIKEMLAAN 315
Cdd:cd14026  191 hDIYSYAIIMWEVLSRkIPFEEVTNPLQIMYS-VSQGHRPDTGEDSLpVDIPHRATLI------------NLIESGWAQN 257

                 ....*
gi 119628251 316 PQDRP 320
Cdd:cd14026  258 PDERP 262
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
11-341 4.34e-12

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 65.48  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENvelalrefwalsSIKSQHPNVIHLEECilqkdgmvqkmshgsnS 90
Cdd:cd06641    9 LEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAED------------EIEDIQQEITVLSQC----------------D 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLqlveTSLKGEIAFDPRsayyLWFVMDFCDGGDMNEyLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd06641   61 SPYV----TKYYGSYLKDTK----LWIIMEYLGGGSALD-LLEPGPLDETQIATILrEILKGLDYLHSEKKIHRDIKAAN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISQtrldtsdlEPTLKVADFGLskvcsaSGQNPEEPVSVNkcflsTACGTDFYMAPEVW-EGHYTAKADIFALGiiiw 248
Cdd:cd06641  132 VLLSE--------HGEVKLADFGV------AGQLTDTQIKRN-----*FVGTPFWMAPEVIkQSAYDSKADIWSLG---- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 249 amlerITFIDtetkkelLGSYVKQGTEIVPVGEALL---ENPkmelliPVKKKSMNGRMKQLIKEMLAANPQDRPDAFE- 324
Cdd:cd06641  189 -----ITAIE-------LARGEPPHSELHPMKVLFLipkNNP------PTLEGNYSKPLKEFVEACLNKEPSFRPTAKEl 250
                        330
                 ....*....|....*..
gi 119628251 325 LELRLVQIAFKDSSWET 341
Cdd:cd06641  251 LKHKFILRNAKKTSYLT 267
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
8-250 4.70e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 65.78  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVE-LALREFWALSSIKsqHPNVIHLEECIlqkdgmvqkmsH 86
Cdd:cd07872    8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPcTAIREVSLLKDLK--HANIVTLHDIV-----------H 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNS-SLYLQLVETSLKGeiafdprsayylwfVMDFCdGGDMNEYllsrkpNRKTntsFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd07872   75 TDKSlTLVFEYLDKDLKQ--------------YMDDC-GNIMSMH------NVKI---FLYQILRGLAYCHRRKVLHRDL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEG--HYTAKADIFAL 243
Cdd:cd07872  131 KPQNLLINE--------RGELKLADFGLARAKSVPTKT-----------YSNEVVTLWYRPPDVLLGssEYSTQIDMWGV 191

                 ....*..
gi 119628251 244 GIIIWAM 250
Cdd:cd07872  192 GCIFFEM 198
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
2-248 4.71e-12

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 65.52  E-value: 4.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   2 VSSQPKYDLIRE-------VGRGSYGVVYEAVIRKTSAR------VAVKKIRCHAPENvELA--LREFWALSSIkSQHPN 66
Cdd:cd05053    1 LPLDPEWELPRDrltlgkpLGEGAFGQVVKAEAVGLDNKpnevvtVAVKMLKDDATEK-DLSdlVSEMEMMKMI-GKHKN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  67 VIHLEECILQKDgmvqkmshgsnsslylqlvetslkgeiafdPrsayyLWFVMDFCDGGDMNEYLLSRKP---------- 136
Cdd:cd05053   79 IINLLGACTQDG------------------------------P-----LYVVVEYASKGNLREFLRARRPpgeeaspddp 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 137 -------NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKvcsasgqnpeepvS 209
Cdd:cd05053  124 rvpeeqlTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE--------DNVMKIADFGLAR-------------D 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119628251 210 VNKCflstacgtDFY------------MAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05053  183 IHHI--------DYYrkttngrlpvkwMAPEaLFDRVYTHQSDVWSFGVLLW 226
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
8-271 5.02e-12

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 66.18  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVyEAVIRKTSARVAVKKIRchapENVELALRE----FWALSSIKS--QHPNVIHLEeCILQKDGmv 81
Cdd:cd05621   54 YDVVKVIGRGAFGEV-QLVRHKASQKVYAMKLL----SKFEMIKRSdsafFWEERDIMAfaNSPWVVQLF-CAFQDDK-- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd05621  126 --------------------------------YLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGqnpeepvsVNKCflSTACGTDFYMAPEVW-----EGHYTA 236
Cdd:cd05621  174 HRDVKPDNMLL--------DKYGHLKLADFGTCMKMDETG--------MVHC--DTAVGTPDYISPEVLksqggDGYYGR 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 119628251 237 KADIFALGIIIWAMLERITFIDTETkkeLLGSYVK 271
Cdd:cd05621  236 ECDWWSVGVFLFEMLVGDTPFYADS---LVGTYSK 267
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
152-255 5.10e-12

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 65.60  E-value: 5.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 152 LAFLHKNQIIHRDLKPDNILISQTRLDtsdleptlKVADFGLSKVCSASGQNpeepvsvnkCFLSTACGTDFYMAPEVWE 231
Cdd:cd14158  130 INYLHENNHIHRDIKSANILLDETFVP--------KISDFGLARASEKFSQT---------IMTERIVGTTAYMAPEALR 192
                         90       100
                 ....*....|....*....|....
gi 119628251 232 GHYTAKADIFALGIIiwaMLERIT 255
Cdd:cd14158  193 GEITPKSDIFSFGVV---LLEIIT 213
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
14-247 5.16e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 65.12  E-value: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKK----IRCHAPENveLALREFWAlSSIKSQHPNVIHLEECILQKDGMVqkmshgsn 89
Cdd:cd14051    8 IGSGEFGSVYKCINRLDGCVYAIKKskkpVAGSVDEQ--NALNEVYA-HAVLGKHPHVVRYYSAWAEDDHMI-------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 sslylqlvetsLKGEiafdprsayylwfvmdFCDGGDMNEYLLSrkpNRKTNTSF--------MLQLSSALAFLHKNQII 161
Cdd:cd14051   77 -----------IQNE----------------YCNGGSLADAISE---NEKAGERFseaelkdlLLQVAQGLKYIHSQNLV 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQTR----------------LDTSDLEPTLKVADFGlsKVCSASGQNPEEpvsvnkcflstacGTDFYM 225
Cdd:cd14051  127 HMDIKPGNIFISRTPnpvsseeeeedfegeeDNPESNEVTYKIGDLG--HVTSISNPQVEE-------------GDCRFL 191
                        250       260
                 ....*....|....*....|....
gi 119628251 226 APEVWEGHYT--AKADIFALGIII 247
Cdd:cd14051  192 ANEILQENYShlPKADIFALALTV 215
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
14-251 5.55e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 65.07  E-value: 5.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELAlREFWALSSIKSQHPNVIHleECILQKDGMVQkmshgsnssly 93
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVQ-FDPESPETS-KEVNALECEIQLLKNLLH--ERIVQYYGCLR----------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafDPRSAYyLWFVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd06652   75 --------------DPQERT-LSIFMEYMPGGSIKDQLksygaLTENVTRK----YTRQILEGVHYLHSNMIVHRDIKGA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILisqtrldtSDLEPTLKVADFGLSK----VC-SASGqnpeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIFA 242
Cdd:cd06652  136 NIL--------RDSVGNVKLGDFGASKrlqtIClSGTG-------------MKSVTGTPYWMSPEVISGEgYGRKADIWS 194

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd06652  195 VGCTVVEML 203
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
8-266 5.69e-12

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 65.02  E-value: 5.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKI---------RCHAPENVElalREFWALSSIksQHPNVIHLEECILQKD 78
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIkkrrlsssrRGVSREEIE---REVNILREI--QHPNIITLHDIFENKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 GMVqkmshgsnssLYLQLVEtslkgeiafdprsayylwfvmdfcdGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHK 157
Cdd:cd14195   82 DVV----------LILELVS-------------------------GGELFDFLAEKESlTEEEATQFLKQILDGVHYLHS 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWEGHYTA- 236
Cdd:cd14195  127 KRIAHFDLKPENIML----LDKNVPNPRIKLIDFGIAHKIEAGNE------------FKNIFGTPEFVAPEIVNYEPLGl 190
                        250       260       270
                 ....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14195  191 EADMWSIGVITYILLSGASPFLGETKQETL 220
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
10-332 5.81e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 65.42  E-value: 5.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVV----YEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEecilqkdGMVqkMS 85
Cdd:cd14205    8 FLQQLGKGNFGSVemcrYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSL--QHDNIVKYK-------GVC--YS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSNSslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLlsRKPNRKTNTSFMLQLSS----ALAFLHKNQII 161
Cdd:cd14205   77 AGRRN------------------------LRLIMEYLPYGSLRDYL--QKHKERIDHIKLLQYTSqickGMEYLGTKRYI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQ-----NP-EEPVsvnkcflstacgtdFYMAPE-VWEGHY 234
Cdd:cd14205  131 HRDLATRNILVEN--------ENRVKIGDFGLTKVLPQDKEyykvkEPgESPI--------------FWYAPEsLTESKF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 TAKADIFALGIIIWamlERITFIDTETKK-----ELLGSYvKQGTEIVPVGEALLENpkmellipvkkksmNGRMKQ--- 306
Cdd:cd14205  189 SVASDVWSFGVVLY---ELFTYIEKSKSPpaefmRMIGND-KQGQMIVFHLIELLKN--------------NGRLPRpdg 250
                        330       340       350
                 ....*....|....*....|....*....|...
gi 119628251 307 -------LIKEMLAANPQDRPDAFELELRLVQI 332
Cdd:cd14205  251 cpdeiymIMTECWNNNVNQRPSFRDLALRVDQI 283
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
115-316 5.99e-12

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 65.44  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH-----------KNQIIHRDLKPDNILISqtrldtSDLe 183
Cdd:cd14140   68 LWLITAFHDKGSLTDYLKGNIVSWNELCHIAETMARGLSYLHedvprckgeghKPAIAHRDFKSKNVLLK------NDL- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 184 pTLKVADFGLSkVCSASGQNPEEPvsvnkcflSTACGTDFYMAPEVWEGHYT------AKADIFALGIIIWAMLERITFI 257
Cdd:cd14140  141 -TAVLADFGLA-VRFEPGKPPGDT--------HGQVGTRRYMAPEVLEGAINfqrdsfLRIDMYAMGLVLWELVSRCKAA 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 258 DTETKKELLgsyvkqgteivPVGEALLENPKMELL--IPVKKKsmngrMKQLIKEMLAANP 316
Cdd:cd14140  211 DGPVDEYML-----------PFEEEIGQHPSLEDLqeVVVHKK-----MRPVFKDHWLKHP 255
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7-247 9.01e-12

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 65.11  E-value: 9.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVK----KIRCHAPENVEL----ALREfwalsSIKSQHPNVIHLEEcilqkd 78
Cdd:cd14225   44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKiirnKKRFHHQALVEVkildALRR-----KDRDNSHNVIHMKE------ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGD---MNEYLLSRKPN---------RKtntsFML 146
Cdd:cd14225  113 -----------------------------------YFYFRNHLCITFEllgMNLYELIKKNNfqgfslsliRR----FAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILISQtRLDTSdleptLKVADFGLSkvcsasgqnpeepvsvnkCF----LSTACGTD 222
Cdd:cd14225  154 SLLQCLRLLYRERIIHCDLKPENILLRQ-RGQSS-----IKVIDFGSS------------------CYehqrVYTYIQSR 209
                        250       260
                 ....*....|....*....|....*.
gi 119628251 223 FYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd14225  210 FYRSPEVILGLpYSMAIDMWSLGCIL 235
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
11-252 9.02e-12

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 64.75  E-value: 9.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRKTSARVAVKKIRchapenvelalrefwalSSIKSQHpnvihleecilQKDgMVQKMSHGSNS 90
Cdd:cd06617    6 IEELGRGAYGVVDKMRHVPTGTIMAVKRIR-----------------ATVNSQE-----------QKR-LLMDLDISMRS 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLQLVEtslkgeiafdprsaYY--------LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM----LQLSSALAFLHKN 158
Cdd:cd06617   57 VDCPYTVT--------------FYgalfregdVWICMEVMDTSLDKFYKKVYDKGLTIPEDILgkiaVSIVKALEYLHSK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 -QIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLskvcsaSGQnpeepvSVNKCFLSTACGTDFYMAPEVWEG----- 232
Cdd:cd06617  123 lSVIHRDVKPSNVLI--------NRNGQVKLCDFGI------SGY------LVDSVAKTIDAGCKPYMAPERINPelnqk 182
                        250       260
                 ....*....|....*....|
gi 119628251 233 HYTAKADIFALGIiiwAMLE 252
Cdd:cd06617  183 GYDVKSDVWSLGI---TMIE 199
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
120-254 9.29e-12

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 64.42  E-value: 9.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 120 DFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtSDLEPTLKVADFGLS-KVC 197
Cdd:cd14155   68 EYINGGNLEQLLDSNEPlSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKR-----DENGYTAVVGDFGLAeKIP 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 198 SASGQNPEEPVsvnkcflstaCGTDFYMAPEVWEGH-YTAKADIFALGIIIWAMLERI 254
Cdd:cd14155  143 DYSDGKEKLAV----------VGSPYWMAPEVLRGEpYNEKADVFSYGIILCEIIARI 190
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
15-320 9.62e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 64.21  E-value: 9.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIRchapeNVElalREFWALSSIksQHPNVIHLEECILQ--KDGMVQKmsHGSNSSL 92
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL-----KIE---KEAEILSVL--SHRNIIQFYGAILEapNYGIVTE--YASYGSL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 YlQLVETSLKGEIAFDprsaYYLWFVMDFCDGgdMNeYLLSRKPNRktntsfmlqlssalaflhknqIIHRDLKPDNILI 172
Cdd:cd14060   70 F-DYLNSNESEEMDMD----QIMTWATDIAKG--MH-YLHMEAPVK---------------------VIHRDLKSRNVVI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 sqtrldTSDLepTLKVADFGLSKVcsasgqnpeepvsVNKCFLSTACGTDFYMAPEVWEGHYTAK-ADIFALGIIIWAML 251
Cdd:cd14060  121 ------AADG--VLKICDFGASRF-------------HSHTTHMSLVGTFPWMAPEVIQSLPVSEtCDTYSYGVVLWEML 179
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 252 ER-ITFidtetkkellgsyvkQGTEIVPVGEALLENPKmELLIPvkkKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14060  180 TReVPF---------------KGLEGLQVAWLVVEKNE-RPTIP---SSCPRSFAELMRRCWEADVKERP 230
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
12-333 1.09e-11

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 64.45  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIkSQHPNVIhleecilqkdgmvqkmshgsnss 91
Cdd:cd14036    6 RVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKL-SGHPNIV----------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lylQLVETSLKGEIAFDPRSAYYLwFVMDFCDGG--DMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQ--IIHRDLK 166
Cdd:cd14036   62 ---QFCSAASIGKEESDQGQAEYL-LLTELCKGQlvDFVKKVEAPGPfSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQtrldtsdlEPTLKVADFGlskvcSASGQ--NPEEPVSVNKCFLS----TACGTDFYMAPEVWEGH----YTA 236
Cdd:cd14036  138 IENLLIGN--------QGQIKLCDFG-----SATTEahYPDYSWSAQKRSLVedeiTRNTTPMYRTPEMIDLYsnypIGE 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 237 KADIFALGIIIWAMLERI-TFIDTETKKELLGSYvkqgteivpvgeALLENPkmellipvKKKSMngrMKQLIKEMLAAN 315
Cdd:cd14036  205 KQDIWALGCILYLLCFRKhPFEDGAKLRIINAKY------------TIPPND--------TQYTV---FHDLIRSTLKVN 261
                        330
                 ....*....|....*...
gi 119628251 316 PQDRPDAFELELRLVQIA 333
Cdd:cd14036  262 PEERLSITEIVEQLQELA 279
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
8-196 1.19e-11

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 64.90  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRchapenvelalrefwalssiKSQHPNvihleecilqkDGMVQKMSHG 87
Cdd:cd05610    6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVK--------------------KADMIN-----------KNMVHQVQAE 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSslyLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYL-LSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd05610   55 RDA---LALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLhIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLK 131
                        170       180       190
                 ....*....|....*....|....*....|
gi 119628251 167 PDNILISQtrldtsdlEPTLKVADFGLSKV 196
Cdd:cd05610  132 PDNMLISN--------EGHIKLTDFGLSKV 153
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
7-266 1.29e-11

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 64.11  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVeLALREFWALSsiKSQHPNVIHLEEcilqkdgmvqkmsh 86
Cdd:cd14104    1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQV-LVKKEISILN--IARHRNILRLHE-------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiAFDprSAYYLWFVMDFCDGGDMNEYLLSRK--PNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14104   64 -------------------SFE--SHEELVMIFEFISGVDIFERITTARfeLNEREIVSYVRQVCEALEFLHSKNIGHFD 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNIlISQTRLDTsdlepTLKVADFGLSkvCSAS-GQNpeepvsVNKCFLSTAcgtdfYMAPEVWEGHYTAKA-DIFA 242
Cdd:cd14104  123 IRPENI-IYCTRRGS-----YIKIIEFGQS--RQLKpGDK------FRLQYTSAE-----FYAPEVHQHESVSTAtDMWS 183
                        250       260
                 ....*....|....*....|....
gi 119628251 243 LGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14104  184 LGCLVYVLLSGINPFEAETNQQTI 207
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
115-251 1.32e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 64.40  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrLDTSDlEPTLKVADFGL 193
Cdd:cd14171   84 LLIVMELMEGGELFDRISQHRHfTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLL----KDNSE-DAPIKLCDFGF 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 194 SKVCSASGQNPEepvsvnkcFlstacgTDFYMAPEVWEGH------------------YTAKADIFALGIIIWAML 251
Cdd:cd14171  159 AKVDQGDLMTPQ--------F------TPYYVAPQVLEAQrrhrkersgiptsptpytYDKSCDMWSLGVIIYIML 220
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
53-251 1.35e-11

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 63.89  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  53 EFWALSSIKSQHPNVIHLEECILQKDGM-VQKMSHGSNSSL-------YLQLVETslkgeiaFDPRSAYYLWfvMDFCDG 124
Cdd:cd14088   13 EFCEIFRAKDKTTGKLYTCKKFLKRDGRkVRKAAKNEINILkmvkhpnILQLVDV-------FETRKEYFIF--LELATG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 125 GDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNiLISQTRLDTSdlepTLKVADFGLSKVCSASGQN 203
Cdd:cd14088   84 REVFDWILDQGYYSERDTSNVIrQVLEAVAYLHSLKIVHRNLKLEN-LVYYNRLKNS----KIVISDFHLAKLENGLIKE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119628251 204 PeepvsvnkcflstaCGTDFYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd14088  159 P--------------CGTPEYLAPEvVGRQRYGRPVDCWAIGVIMYILL 193
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
7-250 1.37e-11

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 63.94  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLirEVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHleecilqkdgmvqkmsh 86
Cdd:cd14032    4 KFDI--ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVR----------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslYLQLVETSLKGEIAfdprsayyLWFVMDFCDGGDMNEYLLSRKPNR-KTNTSFMLQLSSALAFLHKNQ--IIHR 163
Cdd:cd14032   65 ------FYDFWESCAKGKRC--------IVLVTELMTSGTLKTYLKRFKVMKpKVLRSWCRQILKGLLFLHTRTppIIHR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsdlePT--LKVADFGLSKVCSASgqnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTAKADIF 241
Cdd:cd14032  131 DLKCDNIFITG---------PTgsVKIGDLGLATLKRAS-------------FAKSVIGTPEFMAPEMYEEHYDESVDVY 188

                 ....*....
gi 119628251 242 ALGIIIWAM 250
Cdd:cd14032  189 AFGMCMLEM 197
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
7-319 1.43e-11

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 64.20  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKI------------RCHAPENVELAlrefwalssiKSQHPNVIHLEECI 74
Cdd:cd14200    1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLskkkllkqygfpRRPPPRGSKAA----------QGEQAKPLAPLERV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  75 LQKDGMVQKMSHGSnsslYLQLVETslkgeiaFDPRSAYYLWFVMDFCDGGDMNEyLLSRKPNRKTNTSFMLQ-LSSALA 153
Cdd:cd14200   71 YQEIAILKKLDHVN----IVKLIEV-------LDDPAEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRdIVLGIE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 154 FLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSkvcsasgqNPEEPvsvNKCFLSTACGTDFYMAPEVWEGH 233
Cdd:cd14200  139 YLHYQKIVHRDIKPSNLLLGD--------DGHVKIADFGVS--------NQFEG---NDALLSSTAGTPAFMAPETLSDS 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 ---YTAKA-DIFALGIIIWAML-ERITFIDtetkKELLGSYVKQGTEIVPVGEallenpkmellipvkKKSMNGRMKQLI 308
Cdd:cd14200  200 gqsFSGKAlDVWAMGVTLYCFVyGKCPFID----EFILALHNKIKNKPVEFPE---------------EPEISEELKDLI 260
                        330
                 ....*....|.
gi 119628251 309 KEMLAANPQDR 319
Cdd:cd14200  261 LKMLDKNPETR 271
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
114-251 1.46e-11

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 64.68  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEyLLSRKPNRKTN--TSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVAD 190
Cdd:cd05597   75 YLYLVMDYYCGGDLLT-LLSKFEDRLPEemARFYLaEMVLAIDSIHQLGYVHRDIKPDNVLL--------DRNGHIRLAD 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 191 FGL-------SKVCSasgqnpeepvsvnkcflSTACGTDFYMAPEVWE------GHYTAKADIFALGIIIWAML 251
Cdd:cd05597  146 FGSclklredGTVQS-----------------SVAVGTPDYISPEILQamedgkGRYGPECDWWSLGVCMYEML 202
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
14-246 1.54e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 64.40  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALRE--------FWALSSIKS----QHPNVIHLEECILQKDgmv 81
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQlvgmcgihFTTLRELKImneiKHENIMGLVDVYVEGD--- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshgsnsslylqlvetslkgeiafdprsayYLWFVMDFCDGGdmneylLSRKPNRKTNTS------FMLQLSSALAFL 155
Cdd:PTZ00024  94 --------------------------------FINLVMDIMASD------LKKVVDRKIRLTesqvkcILLQILNGLNVL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKC---FLSTACGTDFYMAPEVWEG 232
Cdd:PTZ00024 136 HKWYFMHRDLSPANIFI--------NSKGICKIADFGLARRYGYPPYSDTLSKDETMQrreEMTSKVVTLWYRAPELLMG 207
                        250
                 ....*....|....*.
gi 119628251 233 --HYTAKADIFALGII 246
Cdd:PTZ00024 208 aeKYHFAVDMWSVGCI 223
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
13-250 1.60e-11

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 63.52  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSAR---VAVK---KIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKD-GMVQKMS 85
Cdd:cd05040    2 KLGDGSFGVVRRGEWTTPSGKviqVAVKclkSDVLSQPNAMDDFLKEVNAMHSL--DHPNLIRLYGVVLSSPlMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSnsSLYLQLVEtslkgeiafdpRSAYYLwfVMDFCDggdmneyllsrkpnrktntsFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05040   80 PLG--SLLDRLRK-----------DQGHFL--ISTLCD--------------------YAVQIANGMAYLESKRFIHRDL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdleptLKVADFGLSKvcsASGQNPEEPVSVNKCFLSTAcgtdfYMAPEVWE-GHYTAKADIFALG 244
Cdd:cd05040  125 AARNILLASKDK--------VKIGDFGLMR---ALPQNEDHYVMQEHRKVPFA-----WCAPESLKtRKFSHASDVWMFG 188

                 ....*.
gi 119628251 245 IIIWAM 250
Cdd:cd05040  189 VTLWEM 194
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
114-251 1.75e-11

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 63.77  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDfCDGGDMNEyLLSRKPNRKTNTSF-------MLQlssALAFLHKNQIIHRDLKPDNILISQTRldtsdleptL 186
Cdd:cd14131   76 YLYMVME-CGEIDLAT-ILKKKRPKPIDPNFiryywkqMLE---AVHTIHEEGIVHSDLKPANFLLVKGR---------L 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 187 KVADFGLSKvcsasgQNPEEPVSVNKcflSTACGTDFYMAPE-VWEGHYTA----------KADIFALGIIIWAML 251
Cdd:cd14131  142 KLIDFGIAK------AIQNDTTSIVR---DSQVGTLNYMSPEaIKDTSASGegkpkskigrPSDVWSLGCILYQMV 208
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
14-251 1.86e-11

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 63.32  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRktSARVAVKKIRCHA---PENVELALREFWALSSIksQHPNVIhleecilqkdgmvqkmshgsns 90
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIKRYRANTycsKSDVDMFCREVSILCRL--NHPCVI---------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 slylQLVETSLKgeiafDPrSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSA--LAFLHK--NQIIHRDLK 166
Cdd:cd14064   55 ----QFVGACLD-----DP-SQFAI--VTQYVSGGSLFSLLHEQKRVIDLQSKLIIAVDVAkgMEYLHNltQPIIHRDLN 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILIsqtrldtsDLEPTLKVADFGLSK-VCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWE--GHYTAKADIFAL 243
Cdd:cd14064  123 SHNILL--------YEDGHAVVADFGESRfLQSLDEDN-----------MTKQPGNLRWMAPEVFTqcTRYSIKADVFSY 183

                 ....*...
gi 119628251 244 GIIIWAML 251
Cdd:cd14064  184 ALCLWELL 191
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
114-251 2.32e-11

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 64.26  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEyLLSRKPNR---KTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVAD 190
Cdd:cd05624  146 YLYLVMDYYVGGDLLT-LLSKFEDKlpeDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL--------DMNGHIRLAD 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 191 FGlskvcSASGQNPEEPVSVnkcflSTACGTDFYMAPEVWE------GHYTAKADIFALGIIIWAML 251
Cdd:cd05624  217 FG-----SCLKMNDDGTVQS-----SVAVGTPDYISPEILQamedgmGKYGPECDWWSLGVCMYEML 273
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
74-318 2.37e-11

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 63.89  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDGMVQK--MSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFM-LQLSS 150
Cdd:cd05594   57 ILKKEVIVAKdeVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYgAEIVS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ALAFLH-KNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEV 229
Cdd:cd05594  137 ALDYLHsEKNVVYRDLKLENLML--------DKDGHIKITDFGLCKEGIKDGAT-----------MKTFCGTPEYLAPEV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 230 WEGH-YTAKADIFALGIIIWAML-ERITFIDTETKK--ELLgsyvkqgteivpvgeaLLENPKM-ELLIPVKKKSMNGRM 304
Cdd:cd05594  198 LEDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHEKlfELI----------------LMEEIRFpRTLSPEAKSLLSGLL 261
                        250
                 ....*....|....
gi 119628251 305 KQLIKEMLAANPQD 318
Cdd:cd05594  262 KKDPKQRLGGGPDD 275
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
12-275 2.39e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 63.50  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVELALREFWALSSIKSQHpnVIHLEECILQKDGMVQKMSHGS 88
Cdd:cd05630    6 RVLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEAMALNEKQILEKVNSRF--VVSLAYAYETKDALCLVLTLMN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETslkGEIAFD-PRSAYYlwfVMDFCDGgdmneyllsrkpnrktntsfmlqlssaLAFLHKNQIIHRDLKP 167
Cdd:cd05630   84 GGDLKFHIYHM---GQAGFPeARAVFY---AAEICCG---------------------------LEDLHRERIVYRDLKP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILIsqtrldtsDLEPTLKVADFGLSkVCSASGQNPEEPVsvnkcflstacGTDFYMAPEVWEGH-YTAKADIFALGII 246
Cdd:cd05630  131 ENILL--------DDHGHIRISDLGLA-VHVPEGQTIKGRV-----------GTVGYMAPEVVKNErYTFSPDWWALGCL 190
                        250       260       270
                 ....*....|....*....|....*....|..
gi 119628251 247 IWAMLERITFIDTETKK---ELLGSYVKQGTE 275
Cdd:cd05630  191 LYEMIAGQSPFQQRKKKikrEEVERLVKEVPE 222
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
11-325 2.54e-11

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 63.25  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRK-----TSARVAVKKIRCHAPENVELALREFWALSSiKSQHPNVIHLeecilqkdgmvqkms 85
Cdd:cd05046   10 ITTLGRGEFGEVFLAKAKGieeegGETLVLVKALQKTKDENLQSEFRRELDMFR-KLSHKNVVRL--------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslyLQLVetslkgeiafdpRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML----------QLSSALAFL 155
Cdd:cd05046   74 --------LGLC------------REAEPHYMILEYTDLGDLKQFLRATKSKDEKLKPPPLstkqkvalctQIALGMDHL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKvcsasgqnpeEPVSVNKCFLSTACGTDFYMAPE-VWEGHY 234
Cdd:cd05046  134 SNARFVHRDLAARNCLVSSQRE--------VKVSLLSLSK----------DVYNSEYYKLRNALIPLRWLAPEaVQEDDF 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 235 TAKADIFALGIIIWAMleritFIDTEtkkelLGSYVKQGTEIVpvgeALLENPKMELLIPVKKKSmngRMKQLIKEMLAA 314
Cdd:cd05046  196 STKSDVWSFGVLMWEV-----FTQGE-----LPFYGLSDEEVL----NRLQAGKLELPVPEGCPS---RLYKLMTRCWAV 258
                        330
                 ....*....|.
gi 119628251 315 NPQDRPDAFEL 325
Cdd:cd05046  259 NPKDRPSFSEL 269
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
5-266 2.96e-11

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 63.49  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAV-IRKTSARVAVKKIRcHAPENVELALREFWALSSIKSQHPNVIHLeeCILQKDGMvqk 83
Cdd:cd14214   12 QERYEIVGDLGEGTFGKVVECLdHARGKSQVALKIIR-NVGKYREAARLEINVLKKIKEKDKENKFL--CVLMSDWF--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGSnsslylQLVETSLKGEIAFDprsayylwfvmdFCDGGDMNEYLLsrkpnrkTNTSFM-LQLSSALAFLHKNQIIH 162
Cdd:cd14214   86 NFHGH------MCIAFELLGKNTFE------------FLKENNFQPYPL-------PHIRHMaYQLCHALKFLHENQLTH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLDT-----------SDLEPTLKVADFGlskvcSASGQNPEEpvsvnkcflSTACGTDFYMAPEV-W 230
Cdd:cd14214  141 TDLKPENILFVNSEFDTlynesksceekSVKNTSIRVADFG-----SATFDHEHH---------TTIVATRHYRPPEViL 206
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 119628251 231 EGHYTAKADIFALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14214  207 ELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHL 242
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
8-271 3.27e-11

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 63.87  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVyEAVIRKTSARVAVKKIRchapENVELALRE----FWAlssiksqhpnvihleecilQKDGMVqk 83
Cdd:cd05622   75 YEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLL----SKFEMIKRSdsafFWE-------------------ERDIMA-- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 mshGSNSSLYLQLVetslkgeIAF-DPRsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd05622  129 ---FANSPWVVQLF-------YAFqDDR---YLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIH 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldtsDLEPTLKVADFGlskvcSASGQNPEEPVsvnKCflSTACGTDFYMAPEVW-----EGHYTAK 237
Cdd:cd05622  196 RDVKPDNMLL--------DKSGHLKLADFG-----TCMKMNKEGMV---RC--DTAVGTPDYISPEVLksqggDGYYGRE 257
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119628251 238 ADIFALGIIIWAMLERITFIDTETkkeLLGSYVK 271
Cdd:cd05622  258 CDWWSVGVFLYEMLVGDTPFYADS---LVGTYSK 288
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
145-251 3.30e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.19  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 145 MLQLSSALAFLHKN-QIIHRDLKPDNILISqtrldtSDLEpTLKVADFGLSKVCSASGQNPEEPvsvnkcflsTAC--GT 221
Cdd:cd14001  116 ALSIARALEYLHNEkKILHGDIKSGNVLIK------GDFE-SVKLCDFGVSLPLTENLEVDSDP---------KAQyvGT 179
                         90       100       110
                 ....*....|....*....|....*....|..
gi 119628251 222 DFYMAPEVWE--GHYTAKADIFALGIIIWAML 251
Cdd:cd14001  180 EPWKAKEALEegGVITDKADIFAYGLVLWEMM 211
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
119-247 3.56e-11

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 62.84  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLH-KNQIIHRDLKPDNILIsqtrldTSDLEptLKVADFGLSKv 196
Cdd:cd06620   83 MEYMDCGSLDKILKKKGPfPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILV------NSKGQ--IKLCDFGVSG- 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119628251 197 csasgqnpEEPVSVNKCFLstacGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd06620  154 --------ELINSIADTFV----GTSTYMSPERIQGGkYSVKSDVWSLGLSI 193
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
115-253 3.78e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 62.84  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLlsrkpNRKTNTSF-MLQLS----SALAFLH--------KNQIIHRDLKPDNILISQtrldtsd 181
Cdd:cd14143   68 LWLVSDYHEHGSLFDYL-----NRYTVTVEgMIKLAlsiaSGLAHLHmeivgtqgKPAIAHRDLKSKNILVKK------- 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 182 lEPTLKVADFGLSkVCSASGQNPEEPVSVNKcflstaCGTDFYMAPEVWEG-----HYTA--KADIFALGIIIWAMLER 253
Cdd:cd14143  136 -NGTCCIADLGLA-VRHDSATDTIDIAPNHR------VGTKRYMAPEVLDDtinmkHFESfkRADIYALGLVFWEIARR 206
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
146-337 4.39e-11

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 62.72  E-value: 4.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 146 LQLSSALAFLHKNQ-IIHRDLKPDNILISQTRldtsdlepTLKVADFGLSkvCSASGQNPEEPVSvnkcflstaCGTDF- 223
Cdd:cd14011  121 LQISEALSFLHNDVkLVHGNICPESVVINSNG--------EWKLAGFDFC--ISSEQATDQFPYF---------REYDPn 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 224 ----------YMAPE-VWEGHYTAKADIFALGIIIWAMLERitfidtetkkellGSYVKQGTEIVPVGEALLE---NPKM 289
Cdd:cd14011  182 lpplaqpnlnYLAPEyILSKTCDPASDMFSLGVLIYAIYNK-------------GKPLFDCVNNLLSYKKNSNqlrQLSL 248
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119628251 290 ELLIPVKKKSmngrmKQLIKEMLAANPQDRPDAFELElrlvQIAFKDS 337
Cdd:cd14011  249 SLLEKVPEEL-----RDHVKTLLNVTPEVRPDAEQLS----KIPFFDD 287
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-251 4.80e-11

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 62.34  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAvirKTSARVAVK--KIRCHAPENVELALREFWALSsiKSQHPNVIHLEECILQKD-GMVQKMSH 86
Cdd:cd14150    4 MLKRIGTGSFGTVFRG---KWHGDVAVKilKVTEPTPEQLQAFKNEMQVLR--KTRHVNILLFMGFMTRPNfAIITQWCE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLQLVETSlkgeiaFDprsayylwfVMDFCDggdmneylLSRkpnrktntsfmlQLSSALAFLHKNQIIHRDLK 166
Cdd:cd14150   79 GSSLYRHLHVTETR------FD---------TMQLID--------VAR------------QTAQGMDYLHAKNIIHRDLK 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRldtsdlepTLKVADFGLSKVCSA-SGQNPEEPVSvnkcflstacGTDFYMAPEVWEGH----YTAKADIF 241
Cdd:cd14150  124 SNNIFLHEGL--------TVKIGDFGLATVKTRwSGSQQVEQPS----------GSILWMAPEVIRMQdtnpYSFQSDVY 185
                        250
                 ....*....|
gi 119628251 242 ALGIIIWAML 251
Cdd:cd14150  186 AYGVVLYELM 195
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
15-192 5.08e-11

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 59.76  E-value: 5.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIhleecilqkdgmvqkmshgsnsslyl 94
Cdd:cd13968    2 GEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIP-------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  95 QLVETSLKGEiafdprsayYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQ 174
Cdd:cd13968   56 KVLVTEDVDG---------PNILLMELVKGGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSE 126
                        170
                 ....*....|....*...
gi 119628251 175 TRldtsdlepTLKVADFG 192
Cdd:cd13968  127 DG--------NVKLIDFG 136
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
112-251 5.27e-11

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 62.94  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 112 AYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVAD 190
Cdd:cd05629   73 AQYLYLIMEFLPGGDLMTMLIKYDTFSEDVTRFyMAECVLAIEAVHKLGFIHRDIKPDNILI--------DRGGHIKLSD 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 191 FGLS-----------------KVCSASGQNPEEPVSVNKCFLS-------------------TACGTDFYMAPEVWEGH- 233
Cdd:cd05629  145 FGLStgfhkqhdsayyqkllqGKSNKNRIDNRNSVAVDSINLTmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQQg 224
                        170
                 ....*....|....*...
gi 119628251 234 YTAKADIFALGIIIWAML 251
Cdd:cd05629  225 YGQECDWWSLGAIMFECL 242
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
14-266 5.39e-11

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 62.24  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkmshgsnssly 93
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQL--NHANLIQLYD--------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPN--RKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd14193   69 ------------AFESRNDIVL--VMEYVDGGELFDRIIDENYNltELDTILFIKQICEGIQYMHQMYILHLDLKPENIL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 -ISQTrldtsdlEPTLKVADFGLskvcsASGQNPEEPVSVNkcflstaCGTDFYMAPEVWEGHYTA-KADIFALGIIIWA 249
Cdd:cd14193  135 cVSRE-------ANQVKIIDFGL-----ARRYKPREKLRVN-------FGTPEFLAPEVVNYEFVSfPTDMWSLGVIAYM 195
                        250       260
                 ....*....|....*....|.
gi 119628251 250 MLERIT-FI---DTETKKELL 266
Cdd:cd14193  196 LLSGLSpFLgedDNETLNNIL 216
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
118-325 5.80e-11

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 62.38  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRK-PNRKTNTSFMLQLSSALAFLH--KNQIIHRDLKPDNILISQtrlDTSDLEptLKVADFGLS 194
Cdd:cd14041   89 VLEYCEGNDLDFYLKQHKlMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVN---GTACGE--IKITDFGLS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 195 KVCSASGQNPEEPVSVNkcflSTACGTDFYMAPEVW-----EGHYTAKADIFALGIIIWAMLE-RITFIDTETKKELLgs 268
Cdd:cd14041  164 KIMDDDSYNSVDGMELT----SQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFYQCLYgRKPFGHNQSQQDIL-- 237
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 269 yvkQGTEIVPVGEalLENPKMELLIPvkkksmngRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14041  238 ---QENTILKATE--VQFPPKPVVTP--------EAKAFIRRCLAYRKEDRIDVQQL 281
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
7-250 6.36e-11

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 62.05  E-value: 6.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLirEVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECIlqkdgmvqkmsh 86
Cdd:cd14031   13 KFDI--ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSW------------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvETSLKGEIAfdprsayyLWFVMDFCDGGDMNEYLLSRKPNR-KTNTSFMLQLSSALAFLHKNQ--IIHR 163
Cdd:cd14031   79 -----------ESVLKGKKC--------IVLVTELMTSGTLKTYLKRFKVMKpKVLRSWCRQILKGLQFLHTRTppIIHR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsdlePT--LKVADFGLSKVCSASgqnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTAKADIF 241
Cdd:cd14031  140 DLKCDNIFITG---------PTgsVKIGDLGLATLMRTS-------------FAKSVIGTPEFMAPEMYEEHYDESVDVY 197

                 ....*....
gi 119628251 242 ALGIIIWAM 250
Cdd:cd14031  198 AFGMCMLEM 206
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
118-325 7.38e-11

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 62.00  E-value: 7.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRK-PNRKTNTSFMLQLSSALAFLH--KNQIIHRDLKPDNILIsqtrLDTSDLEpTLKVADFGLS 194
Cdd:cd14040   89 VLEYCEGNDLDFYLKQHKlMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILL----VDGTACG-EIKITDFGLS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 195 KVCSasgqnpEEPVSVNKCFL-STACGTDFYMAPEVW-----EGHYTAKADIFALGIIIWAMLE-RITFIDTETKKELLg 267
Cdd:cd14040  164 KIMD------DDSYGVDGMDLtSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYgRKPFGHNQSQQDIL- 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 268 syvkQGTEIVPVgeallenpkMELLIPVkKKSMNGRMKQLIKEMLAANPQDRPDAFEL 325
Cdd:cd14040  237 ----QENTILKA---------TEVQFPV-KPVVSNEAKAFIRRCLAYRKEDRFDVHQL 280
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
6-248 8.18e-11

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 61.62  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   6 PKYDLIREV-GRGSYGVVYEAVIRKTSAR---VAVKKIRCHAPENvelALREFWALSSIKSQ--HPNVIHLEecilqkdG 79
Cdd:cd05033    3 ASYVTIEKViGGGEFGEVCSGSLKLPGKKeidVAIKTLKSGYSDK---QRLDFLTEASIMGQfdHPNVIRLE-------G 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 MVQKMShgsnsslylqlvetslkgeiafdPrsayyLWFVMDFCDGGDMNEYLlsrkpnRKTNTSF-------MLQ-LSSA 151
Cdd:cd05033   73 VVTKSR-----------------------P-----VMIVTEYMENGSLDKFL------RENDGKFtvtqlvgMLRgIASG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 152 LAFLHKNQIIHRDLKPDNILISqtrldtSDLepTLKVADFGLSKVCSASgqNPEEPVSVNKCFLStacgtdfYMAPE-VW 230
Cdd:cd05033  119 MKYLSEMNYVHRDLAARNILVN------SDL--VCKVSDFGLSRRLEDS--EATYTTKGGKIPIR-------WTAPEaIA 181
                        250
                 ....*....|....*...
gi 119628251 231 EGHYTAKADIFALGIIIW 248
Cdd:cd05033  182 YRKFTSASDVWSFGIVMW 199
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
13-250 8.26e-11

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 61.79  E-value: 8.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRchapenVELALREFwalssiksqhpNVIHLEECILqkdgmvqkmsHGSNSSL 92
Cdd:cd06622    8 ELGKGNYGSVYKVLHRPTGVTMAMKEIR------LELDESKF-----------NQIIMELDIL----------HKAVSPY 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  93 YLQLVEtslkgeiAFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSA----LAFL-HKNQIIHRDLKP 167
Cdd:cd06622   61 IVDFYG-------AFFIEGAVYM--CMEYMDAGSLDKLYAGGVATEGIPEDVLRRITYAvvkgLKFLkEEHNIIHRDVKP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnkcFLSTACGTDFYMAPE-------VWEGHYTAKADI 240
Cdd:cd06622  132 TNVLVNG--------NGQVKLCDFGVSGNLVAS-------------LAKTNIGCQSYMAPEriksggpNQNPTYTVQSDV 190
                        250
                 ....*....|
gi 119628251 241 FALGIIIWAM 250
Cdd:cd06622  191 WSLGLSILEM 200
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
11-320 8.70e-11

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 61.84  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVV----YEAVIRKTSARVAVKKIRCH-APENVELALREFWALSSIksQHPNVIHLEECIlqkdgmvqkmS 85
Cdd:cd05080    9 IRDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADcGPQHRSGWKQEIDILKTL--YHENIVKYKGCC----------S 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05080   77 EQGGKSLQL-----------------------IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdleptLKVADFGLSKVCSAS------GQNPEEPVsvnkcflstacgtdFYMAPE-VWEGHYTAKA 238
Cdd:cd05080  134 AARNVLLDNDRL--------VKIGDFGLAKAVPEGheyyrvREDGDSPV--------------FWYAPEcLKEYKFYYAS 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 239 DIFALGIIIWAMLERITFIDTETKK--ELLGsyVKQG-TEIVPVGEaLLENpKMELLIPvkkKSMNGRMKQLIKEMLAAN 315
Cdd:cd05080  192 DVWSFGVTLYELLTHCDSSQSPPTKflEMIG--IAQGqMTVVRLIE-LLER-GERLPCP---DKCPQEVYHLMKNCWETE 264

                 ....*
gi 119628251 316 PQDRP 320
Cdd:cd05080  265 ASFRP 269
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
10-248 9.93e-11

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 61.62  E-value: 9.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVI-----RKTSARVAVKKIRchapENVELALR-EFWALSSIKS--QHPNVIhleeCILqkdGMV 81
Cdd:cd05048    9 FLEELGEGAFGKVYKGELlgpssEESAISVAIKTLK----ENASPKTQqDFRREAELMSdlQHPNIV----CLL---GVC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKmshgsnSSLYLQLVEtslkgeiafdprsayylwfvmdFCDGGDMNEYLLSRKPNRKTNTS-----------------F 144
Cdd:cd05048   78 TK------EQPQCMLFE----------------------YMAHGDLHEFLVRHSPHSDVGVSsdddgtassldqsdflhI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 145 MLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASgqnpeepvsvnkcflstacgtDFY 224
Cdd:cd05048  130 AIQIAAGMEYLSSHHYVHRDLAARNCLVGDGL--------TVKISDFGLSRDIYSS---------------------DYY 180
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119628251 225 ------------MAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05048  181 rvqsksllpvrwMPPEaILYGKFTTESDVWSFGVVLW 217
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
15-253 1.11e-10

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 61.30  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  15 GRGSYGVVYEAVIrKTSARVAVKKIRCHaPENVELALREFWALSsiksqhpnvihlEECilqkdGMVQKMSHgSNSSLYL 94
Cdd:cd06631   10 GKGAYGTVYCGLT-STGQLIAVKQVELD-TSDKEKAEKEYEKLQ------------EEV-----DLLKTLKH-VNIVGYL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  95 qlvETSLKGEIafdprsayyLWFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILis 173
Cdd:cd06631   70 ---GTCLEDNV---------VSIFMEFVPGGSIASILARFGAlEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIM-- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 174 qtrldtsdLEPT--LKVADFGLSK-VC--SASGQNPEepvsvnkcFLSTACGTDFYMAPEVW-EGHYTAKADIFALGIII 247
Cdd:cd06631  136 --------LMPNgvIKLIDFGCAKrLCinLSSGSQSQ--------LLKSMRGTPYWMAPEVInETGHGRKSDIWSIGCTV 199

                 ....*.
gi 119628251 248 WAMLER 253
Cdd:cd06631  200 FEMATG 205
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
14-255 1.11e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 61.77  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSarVAVKKIRchapENVELA--------LREFWALSSIKsqHPNVIHLEECILQKdgmvqkms 85
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTE--YAVKRLK----EDSELDwsvvknsfLTEVEKLSRFR--HPNIVDLAGYSAQQ-------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hGSNSSLYLQLVETSLKGEIAFDPRSAYYLWfvmdfcdggdmneyllsrkPNRktnTSFMLQLSSALAFLHKNQ--IIHR 163
Cdd:cd14159   65 -GNYCLIYVYLPNGSLEDRLHCQVSCPCLSW-------------------SQR---LHVLLGTARAIQYLHSDSpsLIHG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTrldtsdLEPtlKVADFGLSKVCSaSGQNPEEPVSVNKCflSTACGTDFYMAPE-VWEGHYTAKADIFA 242
Cdd:cd14159  122 DVKSSNILLDAA------LNP--KLGDFGLARFSR-RPKQPGMSSTLART--QTVRGTLAYLPEEyVKTGTLSVEIDVYS 190
                        250
                 ....*....|...
gi 119628251 243 LGIIiwaMLERIT 255
Cdd:cd14159  191 FGVV---LLELLT 200
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-251 1.19e-10

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 61.55  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYeaVIRKTSARVAVKkirchapenvelalrefwaLSSIKsqhpnvihleecILQKDGMVQKMSHG 87
Cdd:cd05613    2 FELLKVLGTGAYGKVF--LVRKVSGHDAGK-------------------LYAMK------------VLKKATIVQKAKTA 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQLVETSLKGEI------AFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTS-FMLQLSSALAFLHKNQI 160
Cdd:cd05613   49 EHTRTERQVLEHIRQSPFlvtlhyAFQTDTKLHL--ILDYINGGELFTHLSQRERFTENEVQiYIGEIVLALEHLHKLGI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNILisqtrLDTSDlepTLKVADFGLSKVCSAsgQNPEEPVSVnkcflstaCGTDFYMAPEVWEGHYTA--KA 238
Cdd:cd05613  127 IYRDIKLENIL-----LDSSG---HVVLTDFGLSKEFLL--DENERAYSF--------CGTIEYMAPEIVRGGDSGhdKA 188
                        250
                 ....*....|....
gi 119628251 239 -DIFALGIIIWAML 251
Cdd:cd05613  189 vDWWSLGVLMYELL 202
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
8-266 1.61e-10

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 60.69  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElALREFWALSSIksQHPNVIHLEEcilqkdgmvqkmshg 87
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTS-ARRELALLAEL--DHKSIVRFHD--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvetslkgeiAFDPRSAyyLWFVMDFCdggdmNEYLLSRKPNRKTN-----TSFMLQLSSALAFLHKNQIIH 162
Cdd:cd14108   66 ------------------AFEKRRV--VIIVTELC-----HEELLERITKRPTVcesevRSYMRQLLEGIEYLHQNDVLH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLDtsdlepTLKVADFGlskvcSASGQNPEEPvsvnkcfLSTACGTDFYMAPE-VWEGHYTAKADIF 241
Cdd:cd14108  121 LDLKPENLLMADQKTD------QVRICDFG-----NAQELTPNEP-------QYCKYGTPEFVAPEiVNQSPVSKVTDIW 182
                        250       260
                 ....*....|....*....|....*
gi 119628251 242 ALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14108  183 PVGVIAYLCLTGISPFVGENDRTTL 207
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
12-256 1.66e-10

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


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 60.37  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSaRVAVKKIRCHAPENVELaLREfwALSSIKSQHPNVIHL------EECILqkdgMVQK-M 84
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNGTT-KVAVKTLKPGTMSPEAF-LQE--AQIMKKLRHDKLVQLyavcsdEEPIY----IVTElM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSnsslylqlvetslkgeiafdprsayylwfVMDFCDGGDmneyllSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd05034   73 SKGS-----------------------------LLDYLRTGE------GRALRLPQLIDMAAQIASGMAYLESRNYIHRD 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTrldtsdlePTLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDF---YMAPE-VWEGHYTAKADI 240
Cdd:cd05034  118 LAARNILVGEN--------NVCKVADFGLARLIEDDEYTARE-------------GAKFpikWTAPEaALYGRFTIKSDV 176
                        250
                 ....*....|....*.
gi 119628251 241 FALGIIiwaMLERITF 256
Cdd:cd05034  177 WSFGIL---LYEIVTY 189
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
10-248 1.89e-10

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 60.27  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAviRKTSARVAVKKIRChapenvELALREFWALSSI--KSQHPNVIHLEECILqKDGMVQKMSHG 87
Cdd:cd05083   10 LGEIIGEGEFGAVLQG--EYMGQKVAVKNIKC------DVTAQAFLEETAVmtKLQHKNLVRLLGVIL-HNGLYIVMELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSL--YLQLvetslKGEIAFDPrsAYYLWFVMDFCDGgdmNEYLLSRKpnrktntsfmlqlssalaflhknqIIHRDL 165
Cdd:cd05083   81 SKGNLvnFLRS-----RGRALVPV--IQLLQFSLDVAEG---MEYLESKK------------------------LVHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsDLEPtlKVADFGLSKVCSASGQNPEEPVSvnkcflstacgtdfYMAPEVWE-GHYTAKADIFALG 244
Cdd:cd05083  127 AARNILVSE------DGVA--KISDFGLAKVGSMGVDNSRLPVK--------------WTAPEALKnKKFSSKSDVWSYG 184

                 ....
gi 119628251 245 IIIW 248
Cdd:cd05083  185 VLLW 188
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
12-252 1.91e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 60.68  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVY--EAVIRKTSARVAVKKIRCHA-PENVELALREFWALSSIksQHPNVIhleECILQkdgmvqkmshgs 88
Cdd:cd05042    1 QEIGNGWFGKVLlgEIYSGTSVAQVVVKELKASAnPKEQDTFLKEGQPYRIL--QHPNIL---QCLGQ------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslylqLVETSlkgeiafdPrsayYLwFVMDFCDGGDMNEYLLSRKPNRKTNTSFML------QLSSALAFLHKNQIIH 162
Cdd:cd05042   64 -------CVEAI--------P----YL-LVMEFCDLGDLKAYLRSEREHERGDSDTRTlqrmacEVAAGLAHLHKLNFVH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILIsqtrldTSDLepTLKVADFGLSKvcsaSGQNPEEPVSVNKCFLSTAcgtdfYMAPE-VWEGH-------Y 234
Cdd:cd05042  124 SDLALRNCLL------TSDL--TVKIGDYGLAH----SRYKEDYIETDDKLWFPLR-----WTAPElVTEFHdrllvvdQ 186
                        250
                 ....*....|....*...
gi 119628251 235 TAKADIFALGIIIWAMLE 252
Cdd:cd05042  187 TKYSNIWSLGVTLWELFE 204
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
115-251 1.93e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 61.60  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05625   76 LYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIaELTCAVESVHKMGFIHRDIKPDNILI--------DRDGHIKLTDFGL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 skvCSA-----------SGQNPEE-----------PVSV-----------------NKCFLSTACGTDFYMAPEV-WEGH 233
Cdd:cd05625  148 ---CTGfrwthdskyyqSGDHLRQdsmdfsnewgdPENCrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVlLRTG 224
                        170
                 ....*....|....*...
gi 119628251 234 YTAKADIFALGIIIWAML 251
Cdd:cd05625  225 YTQLCDWWSVGVILFEML 242
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
118-322 2.02e-10

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 60.48  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSR--KPNRKTNTSFMLQLSSALAFLHKNQII-HRDLKPDNILIsqtrldtsDLEPTLKVADFGLS 194
Cdd:cd13992   74 VTEYCTRGSLQDVLLNReiKMDWMFKSSFIKDIVKGMNYLHSSSIGyHGRLKSSNCLV--------DSRWVVKLTDFGLR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 195 KVCSASGQNPEEPVSVNKCFLstacgtdfYMAPE-------VWEGhyTAKADIFALGIIIWAMLERITFIDTETKKELLG 267
Cdd:cd13992  146 NLLEEQTNHQLDEDAQHKKLL--------WTAPEllrgsllEVRG--TQKGDVYSFAIILYEILFRSDPFALEREVAIVE 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 268 SYVKQGTEIvpvgeallenPKMELLIPVKKKSMngRMKQLIKEMLAANPQDRPDA 322
Cdd:cd13992  216 KVISGGNKP----------FRPELAVLLDEFPP--RLVLLVKQCWAENPEKRPSF 258
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
106-270 2.11e-10

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 60.36  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 106 AFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTS--FMLQLSSALAFLHKNQIIHRDLKPDNIL-ISQTrldtsdl 182
Cdd:cd14192   69 AFESKTNLTL--IMEYVDGGELFDRITDESYQLTELDAilFTRQICEGVHYLHQHYILHLDLKPENILcVNST------- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 183 EPTLKVADFGLskvcsASGQNPEEPVSVNkcflstaCGTDFYMAPEVWEGHYTA-KADIFALGIIIWAMLERITFIDTET 261
Cdd:cd14192  140 GNQIKIIDFGL-----ARRYKPREKLKVN-------FGTPEFLAPEVVNYDFVSfPTDMWSVGVITYMLLSGLSPFLGET 207

                 ....*....
gi 119628251 262 KKELLGSYV 270
Cdd:cd14192  208 DAETMNNIV 216
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
115-251 2.11e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 60.67  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNrktNTSF--------MLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTL 186
Cdd:cd05608   76 LCLVMTIMNGGDLRYHIYNVDEE---NPGFqepracfyTAQIISGLEHLHQRRIIYRDLKPENVLL--------DDDGNV 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 187 KVADFGLSkVCSASGQNPEEPVSvnkcflstacGTDFYMAPEVWEG-HYTAKADIFALGIIIWAML 251
Cdd:cd05608  145 RISDLGLA-VELKDGQTKTKGYA----------GTPGFMAPELLLGeEYDYSVDYFTLGVTLYEMI 199
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
12-251 2.34e-10

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 60.42  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELAlREFWALssiksqhpnvihleECILQkdgMVQKMSHGSNSS 91
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVP-FDPDSQETS-KEVNAL--------------ECEIQ---LLKNLRHDRIVQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 LYLQLVetslkgeiafDPRSAYYLWFVmDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd06653   69 YYGCLR----------DPEEKKLSIFV-EYMPGGSVKDQLkaygaLTENVTRR----YTRQILQGVSYLHSNMIVHRDIK 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILisqtrldtSDLEPTLKVADFGLSK----VC-SASGqnpeepvsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADI 240
Cdd:cd06653  134 GANIL--------RDSAGNVKLGDFGASKriqtICmSGTG-------------IKSVTGTPYWMSPEVISGEgYGRKADV 192
                        250
                 ....*....|.
gi 119628251 241 FALGIIIWAML 251
Cdd:cd06653  193 WSVACTVVEML 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-320 3.55e-10

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 60.07  E-value: 3.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAvirKTSARVAVKKIRCHAPENVELalrefwalssiksqhpnvihleECILQKDGMVQKMSHGSnss 91
Cdd:cd14151   14 QRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQL----------------------QAFKNEVGVLRKTRHVN--- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  92 lYLQLVETSLKGEIAFdprsayylwfVMDFCDGGDMNEYL--LSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDN 169
Cdd:cd14151   66 -ILLFMGYSTKPQLAI----------VTQWCEGSSLYHHLhiIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILISQtrldtsdlEPTLKVADFGLSKVCSA-SGQNPEEPVSvnkcflstacGTDFYMAPEVW----EGHYTAKADIFALG 244
Cdd:cd14151  135 IFLHE--------DLTVKIGDFGLATVKSRwSGSHQFEQLS----------GSILWMAPEVIrmqdKNPYSFQSDVYAFG 196
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119628251 245 IIIWAMLE-RITFIDTETKKELlgsyvkqgteIVPVGEALLeNPKMELLipvkKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14151  197 IVLYELMTgQLPYSNINNRDQI----------IFMVGRGYL-SPDLSKV----RSNCPKAMKRLMAECLKKKRDERP 258
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
119-265 3.61e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 60.14  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNEYLlsrKPNRKTNTSFMLQLSSA----LAFLH-KNQIIHRDLKPDNILISqtrldtSDLEptLKVADFGL 193
Cdd:cd06615   78 MEHMDGGSLDQVL---KKAGRIPENILGKISIAvlrgLTYLReKHKIMHRDVKPSNILVN------SRGE--IKLCDFGV 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 194 skvcsaSGQNPEepvSVNKCFLstacGTDFYMAPEVWEG-HYTAKADIFALGIIIWAMLERITFIDTETKKEL 265
Cdd:cd06615  147 ------SGQLID---SMANSFV----GTRSYMSPERLQGtHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKEL 206
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
115-332 3.73e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 60.05  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLlsRKPNRKTNTSFMLQLSSALAFLH----------KNQIIHRDLKPDNILISQTRldtsdlep 184
Cdd:cd14220   68 LYLITDYHENGSLYDFL--KCTTLDTRALLKLAYSAACGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNG-------- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 185 TLKVADFGLSKVCSASGQNPEEPvsvnkcfLSTACGTDFYMAPEVWE-----GHYTA--KADIFALGIIIWAMLERItfi 257
Cdd:cd14220  138 TCCIADLGLAVKFNSDTNEVDVP-------LNTRVGTKRYMAPEVLDeslnkNHFQAyiMADIYSFGLIIWEMARRC--- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 258 dteTKKELLGSYVKQGTEIVPVG---EALLENPKMELLIPVKKKSMNG-----RMKQLIKEMLAANPQDRPDAFELELRL 329
Cdd:cd14220  208 ---VTGGIVEEYQLPYYDMVPSDpsyEDMREVVCVKRLRPTVSNRWNSdeclrAVLKLMSECWAHNPASRLTALRIKKTL 284

                 ...
gi 119628251 330 VQI 332
Cdd:cd14220  285 AKM 287
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
11-252 4.07e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 59.58  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVY--EAVIRKTSARVAVKKIRCHAPEnveLALREFWALSS-IKS-QHPNvihleecILQKDGmvqkmsh 86
Cdd:cd14206    2 LQEIGNGWFGKVIlgEIFSDYTPAQVVVKELRVSAGP---LEQRKFISEAQpYRSlQHPN-------ILQCLG------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylQLVETslkgeIAFdprsayylWFVMDFCDGGDMNEYLLSRKP-----------NRKTNTSFMLQLSSALAFL 155
Cdd:cd14206   65 --------LCTET-----IPF--------LLIMEFCQLGDLKRYLRAQRKadgmtpdlptrDLRTLQRMAYEITLGLLHL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILIsqtrldTSDLepTLKVADFGLSKvcsasgQNPEEpvsvnkcflstacgtDFYMAPE-VW---- 230
Cdd:cd14206  124 HKNNYIHSDLALRNCLL------TSDL--TVRIGDYGLSH------NNYKE---------------DYYLTPDrLWiplr 174
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119628251 231 --------EGH-------YTAKADIFALGIIIWAMLE 252
Cdd:cd14206  175 wvapelldELHgnlivvdQSKESNVWSLGVTIWELFE 211
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
5-267 4.19e-10

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 60.03  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVI-RKTSARVAVKKIRcHAPENVELALREFWALSSIKSQHPNVIHLeeCIlqkdGMVQK 83
Cdd:cd14215   11 QERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIK-NVEKYKEAARLEINVLEKINEKDPENKNL--CV----QMFDW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGSNSSLYLQLVETSlkgeiAFDprsayylwFVMDfcdggdmNEYLlsrkPNRKTNTSFM-LQLSSALAFLHKNQIIH 162
Cdd:cd14215   84 FDYHGHMCISFELLGLS-----TFD--------FLKE-------NNYL----PYPIHQVRHMaFQVCQAVKFLHDNKLTH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNIL-----------ISQTRLDTSDLEPTLKVADFGlskvcSASGQNPEEpvsvnkcflSTACGTDFYMAPEV-W 230
Cdd:cd14215  140 TDLKPENILfvnsdyeltynLEKKRDERSVKSTAIRVVDFG-----SATFDHEHH---------STIVSTRHYRAPEViL 205
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119628251 231 EGHYTAKADIFALGIIIWAMLERITFIDTETKKELLG 267
Cdd:cd14215  206 ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLA 242
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
11-329 5.14e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 59.23  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEAVIRK--TSARVAVKKIRCHApenvelalrefwalsSIKSQhpnVIHLEEC----ILQKDGMVQKM 84
Cdd:cd05087    2 LKEIGHGWFGKVFLGEVNSglSSTQVVVKELKASA---------------SVQDQ---MQFLEEAqpyrALQHTNLLQCL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRK------PNRKTNTSFMLQLSSALAFLHKN 158
Cdd:cd05087   64 AQCAEVTPYL----------------------LVMEFCPLGDLKGYLRSCRaaesmaPDPLTLQRMACEVACGLLHLHRN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILIsqtrldTSDLepTLKVADFGLSKvCSasgQNPEEPVSVNKCFLSTAcgtdfYMAPE-VWEGH---- 233
Cdd:cd05087  122 NFVHSDLALRNCLL------TADL--TVKIGDYGLSH-CK---YKEDYFVTADQLWVPLR-----WIAPElVDEVHgnll 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 ---YTAKADIFALGIIIWAMLEritfidtetkkelLGS-----YVKQGTEIVPVGEALLENPKMELLIPVKKKSMNgrmk 305
Cdd:cd05087  185 vvdQTKQSNVWSLGVTIWELFE-------------LGNqpyrhYSDRQVLTYTVREQQLKLPKPQLKLSLAERWYE---- 247
                        330       340
                 ....*....|....*....|....
gi 119628251 306 qlIKEMLAANPQDRPDAFELELRL 329
Cdd:cd05087  248 --VMQFCWLQPEQRPTAEEVHLLL 269
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
14-251 5.93e-10

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 59.21  E-value: 5.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSAR-----VAVKKIRCHA-PENVELALREFWALSSIksQHPNVIHLEECILQKDGMVQKMSHG 87
Cdd:cd05045    8 LGEGEFGKVVKATAFRLKGRagyttVAVKMLKENAsSSELRDLLSEFNLLKQV--NHPHVIKLYGACSQDGPLLLIVEYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSL--YLQL---VETSLKGEIAFDPRSAyylwfvmDFCDGgdmneyllSRKPNRKTNTSFMLQLSSALAFLHKNQIIH 162
Cdd:cd05045   86 KYGSLrsFLREsrkVGPSYLGSDGNRNSSY-------LDNPD--------ERALTMGDLISFAWQISRGMQYLAEMKLVH 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLdtsdleptLKVADFGLSK--------VCSASGQNPEEpvsvnkcflstacgtdfYMAPEVWEGH- 233
Cdd:cd05045  151 RDLAARNVLVAEGRK--------MKISDFGLSRdvyeedsyVKRSKGRIPVK-----------------WMAIESLFDHi 205
                        250
                 ....*....|....*...
gi 119628251 234 YTAKADIFALGIIIWAML 251
Cdd:cd05045  206 YTTQSDVWSFGVLLWEIV 223
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-248 6.13e-10

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 59.00  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRkTSARVAVKKIRchapENVeLALREFW--ALSSIKSQHPNVIHLEecilqkdGMVQKmshg 87
Cdd:cd05059    8 FLKELGSGQFGVVHLGKWR-GKIDVAIKMIK----EGS-MSEDDFIeeAKVMMKLSHPKLVQLY-------GVCTK---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 sNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNT--SFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05059   71 -QRPIFI-----------------------VTEYMANGCLLNYLRERRGKFQTEQllEMCKDVCEAMEYLESNGFIHRDL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRLdtsdleptLKVADFGLSKVCsasgqnpeepvsVNKCFLSTAcGTDF---YMAPEVWE-GHYTAKADIF 241
Cdd:cd05059  127 AARNCLVGEQNV--------VKVSDFGLARYV------------LDDEYTSSV-GTKFpvkWSPPEVFMySKFSSKSDVW 185

                 ....*..
gi 119628251 242 ALGIIIW 248
Cdd:cd05059  186 SFGVLMW 192
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
99-253 6.51e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 59.03  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  99 TSLKGEIAFDPR---SAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH--------KNQIIHRDLKP 167
Cdd:cd14144   49 ENILGFIAADIKgtgSWTQLYLITDYHENGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHteifgtqgKPAIAHRDIKS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQtrldtsdlEPTLKVADFGLskvcsASGQNPE-EPVSVNKcflSTACGTDFYMAPEVWE-----GHYTA--KAD 239
Cdd:cd14144  129 KNILVKK--------NGTCCIADLGL-----AVKFISEtNEVDLPP---NTRVGTKRYMAPEVLDeslnrNHFDAykMAD 192
                        170
                 ....*....|....
gi 119628251 240 IFALGIIIWAMLER 253
Cdd:cd14144  193 MYSFGLVLWEIARR 206
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
7-324 8.25e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 59.27  E-value: 8.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIrCHAPENVELALREFWALSSIKS-QHPNVIHLEECILQKdgmvQKMS 85
Cdd:cd07876   22 RYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKL-SRPFQNQTHAKRAYRELVLLKCvNHKNIISLLNVFTPQ----KSLE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSNSSLYLQLVETSLKGEIAFD---PRSAYYLWfvmdfcdggdmneyllsrkpnrktntsfmlQLSSALAFLHKNQIIH 162
Cdd:cd07876   97 EFQDVYLVMELMDANLCQVIHMEldhERMSYLLY------------------------------QMLCGIKHLHSAGIIH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnkcFLSTA-CGTDFYMAPEVWEG-HYTAKADI 240
Cdd:cd07876  147 RDLKPSNIVVKS--------DCTLKILDFGLARTACTN-------------FMMTPyVVTRYYRAPEVILGmGYKENVDI 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLEritfidtetkkellGSYVKQGTEIVPVGEALLE---NPKMELLipvkkksmnGRMKQLIKEMLAANPQ 317
Cdd:cd07876  206 WSVGCIMGELVK--------------GSVIFQGTDHIDQWNKVIEqlgTPSAEFM---------NRLQPTVRNYVENRPQ 262

                 ....*..
gi 119628251 318 DRPDAFE 324
Cdd:cd07876  263 YPGISFE 269
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
12-253 9.59e-10

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 58.25  E-value: 9.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSAR---VAVKKI-RCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGmvqkmshg 87
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSDGQkihCAVKSLnRITDIEEVEQFLKEGIIMKDF--SHPNVLSLLGICLPSEG-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslyLQLVetslkgeiafdprsayylwfVMDFCDGGDMNEYLLS--RKPNRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05058   71 ------SPLV--------------------VLPYMKHGDLRNFIRSetHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRldtsdlepTLKVADFGLSK-VCSASGQNPEE------PVSvnkcflstacgtdfYMAPEVWEGH-YTAK 237
Cdd:cd05058  125 AARNCMLDESF--------TVKVADFGLARdIYDKEYYSVHNhtgaklPVK--------------WMALESLQTQkFTTK 182
                        250
                 ....*....|....*.
gi 119628251 238 ADIFALGIIIWAMLER 253
Cdd:cd05058  183 SDVWSFGVLLWELMTR 198
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
115-251 1.01e-09

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 58.60  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNeYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFG 192
Cdd:cd05606   73 LCFILDLMNGGDLH-YHLSQHGvfSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL--------DEHGHVRISDLG 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 193 LSkvCSASGQNPEEPVsvnkcflstacGTDFYMAPEVWEG--HYTAKADIFALGIIIWAML 251
Cdd:cd05606  144 LA--CDFSKKKPHASV-----------GTHGYMAPEVLQKgvAYDSSADWFSLGCMLYKLL 191
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
10-256 1.13e-09

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 58.51  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIrKTSARVAVKKIRchapenvelalrefwalssiksqhPNVIHLEeCILQKDGMVQKMSHGSN 89
Cdd:cd05072   11 LVKKLGAGQFGEVWMGYY-NNSTKVAVKTLK------------------------PGTMSVQ-AFLEEANLMKTLQHDKL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 SSLYLQLVETslkgeiafDPrsayyLWFVMDFCDGGDMNEYLLSRKPNR---KTNTSFMLQLSSALAFLHKNQIIHRDLK 166
Cdd:cd05072   65 VRLYAVVTKE--------EP-----IYIITEYMAKGSLLDFLKSDEGGKvllPKLIDFSAQIAEGMAYIERKNYIHRDLR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 167 PDNILISQTRLdtsdleptLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDF---YMAPEVWE-GHYTAKADIFA 242
Cdd:cd05072  132 AANVLVSESLM--------CKIADFGLARVIEDNEYTARE-------------GAKFpikWTAPEAINfGSFTIKSDVWS 190
                        250
                 ....*....|....
gi 119628251 243 LGIIIWamlERITF 256
Cdd:cd05072  191 FGILLY---EIVTY 201
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
12-248 1.22e-09

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 58.65  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAV---IRKTSA--RVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLeecilqkdgmvqkmsh 86
Cdd:cd05055   41 KTLGAGAFGKVVEATaygLSKSDAvmKVAVKMLKPTAHSSEREALMSELKIMSHLGNHENIVNL---------------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqLVETSLKGEIafdprsayylWFVMDFCDGGDMNEYLLSRKPNRKTNT---SFMLQLSSALAFLHKNQIIHR 163
Cdd:cd05055  105 ---------LGACTIGGPI----------LVITEYCCYGDLLNFLRRKRESFLTLEdllSFSYQVAKGMAFLASKNCIHR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQTRLdtsdleptLKVADFGLSKvcsaSGQNPEEPVSVNKCFLSTAcgtdfYMAPE-VWEGHYTAKADIFA 242
Cdd:cd05055  166 DLAARNVLLTHGKI--------VKICDFGLAR----DIMNDSNYVVKGNARLPVK-----WMAPEsIFNCVYTFESDVWS 228

                 ....*.
gi 119628251 243 LGIIIW 248
Cdd:cd05055  229 YGILLW 234
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
14-251 1.29e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 58.17  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRcHAPENVELAlREFWALssiksqhpnvihleECILQkdgMVQKMSHGSNSSLY 93
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVQ-FDPESPETS-KEVSAL--------------ECEIQ---LLKNLQHERIVQYY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVEtslkgeiafdpRSAYYLWFVMDFCDGGDMNEYL-----LSRKPNRKtntsFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd06651   76 GCLRD-----------RAEKTLTIFMEYMPGGSVKDQLkaygaLTESVTRK----YTRQILEGMSYLHSNMIVHRDIKGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILisqtrldtSDLEPTLKVADFGLSKVCsasgqnpeEPVSVNKCFLSTACGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd06651  141 NIL--------RDSAGNVKLGDFGASKRL--------QTICMSGTGIRSVTGTPYWMSPEVISGEgYGRKADVWSLGCTV 204

                 ....
gi 119628251 248 WAML 251
Cdd:cd06651  205 VEML 208
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
7-255 1.36e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 58.14  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLirEVGRGSYGVVYEAVIRKTSARVAVkkirchapenVELALREfwaLSSIKSQHpnvihleecILQKDGMVQKMSH 86
Cdd:cd14030   28 KFDI--EIGRGSFKTVYKGLDTETTVEVAW----------CELQDRK---LSKSERQR---------FKEEAGMLKGLQH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gSNSSLYLQLVETSLKGEIAfdprsayyLWFVMDFCDGGDMNEYLLSRKPNR-KTNTSFMLQLSSALAFLHKNQ--IIHR 163
Cdd:cd14030   84 -PNIVRFYDSWESTVKGKKC--------IVLVTELMTSGTLKTYLKRFKVMKiKVLRSWCRQILKGLQFLHTRTppIIHR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISQtrldtsdlePT--LKVADFGLSKVCSASgqnpeepvsvnkcFLSTACGTDFYMAPEVWEGHYTAKADIF 241
Cdd:cd14030  155 DLKCDNIFITG---------PTgsVKIGDLGLATLKRAS-------------FAKSVIGTPEFMAPEMYEEKYDESVDVY 212
                        250
                 ....*....|....
gi 119628251 242 ALGIiiwAMLERIT 255
Cdd:cd14030  213 AFGM---CMLEMAT 223
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
115-251 1.40e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 58.53  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYL-----LSRKPNRKTNTSFMLqlssALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVA 189
Cdd:cd05633   83 LCFILDLMNGGDLHYHLsqhgvFSEKEMRFYATEIIL----GLEHMHNRFVVYRDLKPANILL--------DEHGHVRIS 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 190 DFGLSkvCSASGQNPEEPVsvnkcflstacGTDFYMAPEVWEG--HYTAKADIFALGIIIWAML 251
Cdd:cd05633  151 DLGLA--CDFSKKKPHASV-----------GTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLL 201
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
14-248 1.47e-09

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 58.27  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVK---KIRCHAPenVELALREFWALSsiKSQHPNVIHL---EEcilqkdgmvqkmshg 87
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKvfnNLSFMRP--LDVQMREFEVLK--KLNHKNIVKLfaiEE--------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqlvETSLKGEIafdprsayylwFVMDFCDGGDM--------NEYLLSRkpnrktnTSFMLQLSSALA---FLH 156
Cdd:cd13988   62 ----------ELTTRHKV-----------LVMELCPCGSLytvleepsNAYGLPE-------SEFLIVLRDVVAgmnHLR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILisqtRLDTSDLEPTLKVADFGLSKVCSASGQnpeepvsvnkcFLSTAcGTDFYMAPEVWE----- 231
Cdd:cd13988  114 ENGIVHRDIKPGNIM----RVIGEDGQSVYKLTDFGAARELEDDEQ-----------FVSLY-GTEEYLHPDMYEravlr 177
                        250       260
                 ....*....|....*....|.
gi 119628251 232 ----GHYTAKADIFALGIIIW 248
Cdd:cd13988  178 kdhqKKYGATVDLWSIGVTFY 198
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
126-247 1.50e-09

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 58.42  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 126 DMNEYLLSRKPNRK-----TNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqTRLDTSDleptLKVADFGlskvcSAs 200
Cdd:cd14212   85 GVNLYELLKQNQFRglslqLIRKFLQQLLDALSVLKDARIIHCDLKPENILL--VNLDSPE----IKLIDFG-----SA- 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119628251 201 gqnpeepvsvnkCF----LSTACGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd14212  153 ------------CFenytLYTYIQSRFYRSPEVLLGLpYSTAIDMWSLGCIA 192
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
94-319 1.60e-09

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 57.99  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLL---SRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNI 170
Cdd:cd05607   56 LEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDLKYHIYnvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 171 LIsqtrldtsDLEPTLKVADFGLSkVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIWA 249
Cdd:cd05607  136 LL--------DDNGNCRLSDLGLA-VEVKEGKP-----------ITQRAGTNGYMAPEILkEESYSYPVDWFAMGCSIYE 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 250 MLE-RITFIDTETKkellgsyvkqgteivpVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd05607  196 MVAgRTPFRDHKEK----------------VSKEELKRRTLEDEVKFEHQNFTEEAKDICRLFLAKKPENR 250
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
118-251 1.61e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 57.94  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlePTLKVADFGLSKV 196
Cdd:PHA03390  87 IMDYIKDGDLFDLLKKEGKLSEAEVKKIIrQLVEALNDLHKHNIIHNDIKLENVLYDRAK-------DRIYLCDYGLCKI 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 197 CSASgqnpeepvsvnkcflSTACGTDFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:PHA03390 160 IGTP---------------SCYDGTLDYFSPEKIKGHnYDVSFDWWAVGVLTYELL 200
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
115-251 1.62e-09

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 58.87  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEyLLSRKPNR---KTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADF 191
Cdd:cd05623  147 LYLVMDYYVGGDLLT-LLSKFEDRlpeDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM--------DMNGHIRLADF 217
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 192 GlskvcsaSGQNPEEPVSVNKcflSTACGTDFYMAPEVWE------GHYTAKADIFALGIIIWAML 251
Cdd:cd05623  218 G-------SCLKLMEDGTVQS---SVAVGTPDYISPEILQamedgkGKYGPECDWWSLGVCMYEML 273
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
83-251 1.94e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 58.14  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGS----NSSLYLQLVETslkGEIAFDPRSAYY------LWFVMDFCDGGDMNEYLLSRKPNRKTNTSF-MLQLSSA 151
Cdd:cd14223   39 KMKQGEtlalNERIMLSLVST---GDCPFIVCMSYAfhtpdkLSFILDLMNGGDLHYHLSQHGVFSEAEMRFyAAEIILG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 152 LAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSkvCSASGQNPEEPVsvnkcflstacGTDFYMAPEVWE 231
Cdd:cd14223  116 LEHMHSRFVVYRDLKPANILL--------DEFGHVRISDLGLA--CDFSKKKPHASV-----------GTHGYMAPEVLQ 174
                        170       180
                 ....*....|....*....|..
gi 119628251 232 G--HYTAKADIFALGIIIWAML 251
Cdd:cd14223  175 KgvAYDSSADWFSLGCMLFKLL 196
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
7-251 2.34e-09

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 57.16  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSA-RVAVKKIRcHAPENVELALREFWALSSIksQHPNVIHLEEcilqkdgmvqkms 85
Cdd:cd14112    4 RFSFGSEIFRGRFSVIVKAVDSTTETdAHCAVKIF-EVSDEASEAVREFESLRTL--QHENVQRLIA------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 hgsnsslylqlvetslkgeiAFDPRSayYLWFVMDFCDGgDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14112   68 --------------------AFKPSN--FAYLVMEKLQE-DVFTRFSSNDYySEEQVATTVRQILDALHYLHFKGIAHLD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTRldtsdlEPTLKVADFGLSKvcsasgqnpeepvSVNKCFLSTACGTDFYMAPEVW--EGHYTAKADIFA 242
Cdd:cd14112  125 VQPDNIMFQSVR------SWQVKLVDFGRAQ-------------KVSKLGKVPVDGDTDWASPEFHnpETPITVQSDIWG 185

                 ....*....
gi 119628251 243 LGIIIWAML 251
Cdd:cd14112  186 LGVLTFCLL 194
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
14-251 2.44e-09

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 57.43  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKT------SARVAVKKIRCHAP--ENVELaLREFWALSSIKsqHPNVIH-LEECILqkdgmvqkm 84
Cdd:cd05044    3 LGSGAFGEVFEGTAKDIlgdgsgETKVAVKTLRKGATdqEKAEF-LKEAHLMSNFK--HPNILKlLGVCLD--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKPNRKTNTSFML--QLSSAL------AFLH 156
Cdd:cd05044   71 ----NDPQYI-----------------------ILELMEGGDLLSYLRAARPTAFTPPLLTLkdLLSICVdvakgcVYLE 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISQTRLDtsdlEPTLKVADFGLSKVCSASGQNPEE-----PVSvnkcflstacgtdfYMAPE-VW 230
Cdd:cd05044  124 DMHFVHRDLAARNCLVSSKDYR----ERVVKIGDFGLARDIYKNDYYRKEgegllPVR--------------WMAPEsLV 185
                        250       260
                 ....*....|....*....|.
gi 119628251 231 EGHYTAKADIFALGIIIWAML 251
Cdd:cd05044  186 DGVFTTQSDVWAFGVLMWEIL 206
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
10-253 2.62e-09

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 57.16  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRK---TSARVAVK--KIRCHAPENVELALREfwALSSIKSQHPNVIhleecilqkdgmvqkm 84
Cdd:cd05035    3 LGKILGEGEFGSVMEAQLKQddgSQLKVAVKtmKVDIHTYSEIEEFLSE--AACMKDFDHPNVM---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylQLVETSLKGEIAFDPRSAYylwFVMDFCDGGDMNEYLLSRK----PNR---KTNTSFMLQLSSALAFLHK 157
Cdd:cd05035   65 ----------RLIGVCFTASDLNKPPSPM---VILPFMKHGDLHSYLLYSRlgglPEKlplQTLLKFMVDIAKGMEYLSN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLS-KVCSAS----GQNPEEPVSvnkcflstacgtdfYMAPE-VWE 231
Cdd:cd05035  132 RNFIHRDLAARNCMLDE--------NMTVCVADFGLSrKIYSGDyyrqGRISKMPVK--------------WIALEsLAD 189
                        250       260
                 ....*....|....*....|..
gi 119628251 232 GHYTAKADIFALGIIIWAMLER 253
Cdd:cd05035  190 NVYTSKSDVWSFGVTMWEIATR 211
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
8-255 2.71e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 56.94  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIksQHPNVIHLEECILQKDGMVQKMSHG 87
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCL--HHPKLVQCVDAFEEKANIVMVLEMV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQLVETslkgeiafdprsayylwfvmDFcdggDMNEyllsrkpnrKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd14191   82 SGGELFERIIDE--------------------DF----ELTE---------RECIKYMRQISEGVEYIHKQGIVHLDLKP 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNIL-ISQTrldtsdlEPTLKVADFGLSKVCSASGQnpeepvsvnkcfLSTACGTDFYMAPEVWegHYTA---KADIFAL 243
Cdd:cd14191  129 ENIMcVNKT-------GTKIKLIDFGLARRLENAGS------------LKVLFGTPEFVAPEVI--NYEPigyATDMWSI 187
                        250
                 ....*....|..
gi 119628251 244 GIIIWAMLERIT 255
Cdd:cd14191  188 GVICYILVSGLS 199
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
14-251 2.73e-09

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 57.14  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIRCHApenveLALREFWALSSIKSqhPNVIHLEecilqkdGMVqkmshgsnssly 93
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEV-----FRAEELMACAGLTS--PRVVPLY-------GAV------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 lqlvetslkgeiafdpRSAYYLWFVMDFCDGGDMNEYL--LSRKPNRKTnTSFMLQLSSALAFLHKNQIIHRDLKPDNIL 171
Cdd:cd13991   68 ----------------REGPWVNIFMDLKEGGSLGQLIkeQGCLPEDRA-LHYLGQALEGLEYLHSRKILHGDVKADNVL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 172 ISQTRLDTSdleptlkVADFGLSKVCSASGQnpeepvsvNKCFLSTAC--GTDFYMAPEVWEGH-YTAKADIFALGIIIW 248
Cdd:cd13991  131 LSSDGSDAF-------LCDFGHAECLDPDGL--------GKSLFTGDYipGTETHMAPEVVLGKpCDAKVDVWSSCCMML 195

                 ...
gi 119628251 249 AML 251
Cdd:cd13991  196 HML 198
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
8-324 3.10e-09

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 56.82  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVyEAVIRKTSarvavkKIRCHAPEnveLALRefwalSSIKSQhpnvIHLEECILQKdgmvqkMSHG 87
Cdd:cd14107    4 YEVKEEIGRGTFGFV-KRVTHKGN------GECCAAKF---IPLR-----SSTRAR----AFQERDILAR------LSHR 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLYLQlvetslkgeiaFDPRSAyyLWFVMDFCDggdmNEYLLSRKPNRKTNTS-----FMLQLSSALAFLHKNQIIH 162
Cdd:cd14107   59 RLTCLLDQ-----------FETRKT--LILILELCS----SEELLDRLFLKGVVTEaevklYIQQVLEGIGYLHGMNILH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNIL-ISQTRLDtsdleptLKVADFGLskvcsASGQNPEEPvsvnkcfLSTACGTDFYMAPE-VWEGHYTAKADI 240
Cdd:cd14107  122 LDIKPDNILmVSPTRED-------IKICDFGF-----AQEITPSEH-------QFSKYGSPEFVAPEiVHQEPVSAATDI 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIWAMLE-RITFIDTETKKELLGsyvkqgteiVPVGEALLENPKMellipvkkKSMNGRMKQLIKEMLAANPQDR 319
Cdd:cd14107  183 WALGVIAYLSLTcHSPFAGENDRATLLN---------VAEGVVSWDTPEI--------THLSEDAKDFIKRVLQPDPEKR 245

                 ....*
gi 119628251 320 PDAFE 324
Cdd:cd14107  246 PSASE 250
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
143-244 3.29e-09

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 57.23  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdlepTLKVADFGlskvcSAS--GQNPEEPVSVNKcflstacg 220
Cdd:cd14135  109 SYAQQLFLALKHLKKCNILHADIKPDNILVNEKKN-------TLKLCDFG-----SASdiGENEITPYLVSR-------- 168
                         90       100
                 ....*....|....*....|....*
gi 119628251 221 tdFYMAPEVWEGH-YTAKADIFALG 244
Cdd:cd14135  169 --FYRAPEIILGLpYDYPIDMWSVG 191
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
11-261 3.39e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 56.86  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVV----YEAVIRKTSARVAVKKIRchaPENVELALREFWALSSIKSqhpNVIHleECILQKDGMVQKmsh 86
Cdd:cd05079    9 IRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLK---PESGGNHIADLKKEIEILR---NLYH--ENIVKYKGICTE--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 GSNSSLYLqlvetslkgeiafdprsayylwfVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd05079   78 DGGNGIKL-----------------------IMEFLPSGSLKEYLPRNKNkiNLKQQLKYAVQICKGMDYLGSRQYVHRD 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQtrldtsdlEPTLKVADFGLSKvcsaSGQNPEEPVSVNKCFLSTAcgtdFYMAPE-VWEGHYTAKADIFAL 243
Cdd:cd05079  135 LAARNVLVES--------EHQVKIGDFGLTK----AIETDKEYYTVKDDLDSPV----FWYAPEcLIQSKFYIASDVWSF 198
                        250
                 ....*....|....*...
gi 119628251 244 GIIIWAMLeriTFIDTET 261
Cdd:cd05079  199 GVTLYELL---TYCDSES 213
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
7-332 3.55e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 56.83  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYdlIREVGRGSYGVV----YEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSiksqhpnvihleeciLQKDGMVQ 82
Cdd:cd05081    7 KY--ISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKA---------------LHSDFIVK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 kmshgsnsslylqlvetsLKGeIAFDP-RSAYYLwfVMDFCDGGDMNEYLlSRKPNRKTNTSFML---QLSSALAFLHKN 158
Cdd:cd05081   70 ------------------YRG-VSYGPgRRSLRL--VMEYLPSGCLRDFL-QRHRARLDASRLLLyssQICKGMEYLGSR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSK---------VCSASGQNPEepvsvnkcflstacgtdFYMAPE- 228
Cdd:cd05081  128 RCVHRDLAARNILVES--------EAHVKIADFGLAKllpldkdyyVVREPGQSPI-----------------FWYAPEs 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 229 VWEGHYTAKADIFALGIIIWamlERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVkKKSMNGRMKQLI 308
Cdd:cd05081  183 LSDNIFSRQSDVWSFGVVLY---ELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPA-PPACPAEVHELM 258
                        330       340
                 ....*....|....*....|....
gi 119628251 309 KEMLAANPQDRPDAFELELRLVQI 332
Cdd:cd05081  259 KLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-329 4.46e-09

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 56.65  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKTSArVAVKKIRchaPENVELAlrEFWALSSI--KSQHPNVIHLEECILQKDGM---VQKM 84
Cdd:cd05068   12 LLRKLGSGQFGEVWEGLWNNTTP-VAVKTLK---PGTMDPE--DFLREAQImkKLRHPKLIQLYAVCTLEEPIyiiTELM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSlYLQLVETSLKGEIAFDPRSayylwfvmdfcdggdmneyllsrkpnrktntsfmlQLSSALAFLHKNQIIHRD 164
Cdd:cd05068   86 KHGSLLE-YLQGKGRSLQLPQLIDMAA-----------------------------------QVASGMAYLESQNYIHRD 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILISQTRldtsdlepTLKVADFGLSKVcsasgqnpeepVSVNKCFLSTAcGTDF---YMAPEVWEGH-YTAKADI 240
Cdd:cd05068  130 LAARNVLVGENN--------ICKVADFGLARV-----------IKVEDEYEARE-GAKFpikWTAPEAANYNrFSIKSDV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 241 FALGIIIwamleritfidtetkkellgsyvkqgTEIVPVGEalLENPKM---ELLIPVKKksmNGRM-------KQLIKE 310
Cdd:cd05068  190 WSFGILL--------------------------TEIVTYGR--IPYPGMtnaEVLQQVER---GYRMpcppncpPQLYDI 238
                        330       340
                 ....*....|....*....|...
gi 119628251 311 MLA---ANPQDRPdAFE-LELRL 329
Cdd:cd05068  239 MLEcwkADPMERP-TFEtLQWKL 260
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
114-251 4.50e-09

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 56.91  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEYLLSRK--PNrKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADF 191
Cdd:PTZ00426 105 YLYLVLEFVIGGEFFTFLRRNKrfPN-DVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL--------DKDGFIKMTDF 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119628251 192 GLSKVCSASgqnpeepvsvnkcfLSTACGTDFYMAPEVW--EGHYTAkADIFALGIIIWAML 251
Cdd:PTZ00426 176 GFAKVVDTR--------------TYTLCGTPEYIAPEILlnVGHGKA-ADWWTLGIFIYEIL 222
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
10-248 5.44e-09

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 56.57  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRKT-----SARVAVKKIRchapENVELALREFW---ALSSIKSQHPNVIhleeCILqkdGMV 81
Cdd:cd05091   10 FMEELGEDRFGKVYKGHLFGTapgeqTQAVAIKTLK----DKAEGPLREEFrheAMLRSRLQHPNIV----CLL---GVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMShgsnsslylqlvetslkgeiafdPRSayylwFVMDFCDGGDMNEYLLSRKPNRKTNTS-----------------F 144
Cdd:cd05091   79 TKEQ-----------------------PMS-----MIFSYCSHGDLHEFLVMRSPHSDVGSTdddktvkstlepadflhI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 145 MLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQ-----NPEEPVSvnkcflstac 219
Cdd:cd05091  131 VTQIAAGMEYLSSHHVVHKDLATRNVLVFD--------KLNVKISDLGLFREVYAADYyklmgNSLLPIR---------- 192
                        250       260       270
                 ....*....|....*....|....*....|
gi 119628251 220 gtdfYMAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05091  193 ----WMSPEaIMYGKFSIDSDIWSYGVVLW 218
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
12-252 6.70e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 56.15  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVELALREFWALSSIKSQHpnVIHLEECILQKDGMVQKMSHGS 88
Cdd:cd05631    6 RVLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEAMALNEKRILEKVNSRF--VVSLAYAYETKDALCLVLTIMN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETslkGEIAFDPRSAyyLWFVMDFCDGgdmneyllsrkpnrktntsfmlqlssaLAFLHKNQIIHRDLKPD 168
Cdd:cd05631   84 GGDLKFHIYNM---GNPGFDEQRA--IFYAAELCCG---------------------------LEDLQRERIVYRDLKPE 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILIsqtrldtsDLEPTLKVADFGLSKvcsasgQNPEEPVsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd05631  132 NILL--------DDRGHIRISDLGLAV------QIPEGET------VRGRVGTVGYMAPEVINNEkYTFSPDWWGLGCLI 191

                 ....*
gi 119628251 248 WAMLE 252
Cdd:cd05631  192 YEMIQ 196
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
5-253 7.01e-09

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 56.08  E-value: 7.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   5 QPKYDLIREVGRGSYGVVYEAVIRK---TSARVAVK--KIRCHAPENVELALREfwALSSIKSQHPNVIhleecilqkdg 79
Cdd:cd05074    8 EQQFTLGRMLGKGEFGSVREAQLKSedgSFQKVAVKmlKADIFSSSDIEEFLRE--AACMKEFDHPNVI----------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  80 mvqkmshgsnsslylQLVETSLKGeiafdpRSAYYL---WFVMDFCDGGDMNEYLL-SRKPNRKTNTS------FMLQLS 149
Cdd:cd05074   75 ---------------KLIGVSLRS------RAKGRLpipMVILPFMKHGDLHTFLLmSRIGEEPFTLPlqtlvrFMIDIA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 150 SALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSaSGQnpeepvsvnkcFLSTACGTDF---YMA 226
Cdd:cd05074  134 SGMEYLSSKNFIHRDLAARNCMLNE--------NMTVCVADFGLSKKIY-SGD-----------YYRQGCASKLpvkWLA 193
                        250       260
                 ....*....|....*....|....*...
gi 119628251 227 PE-VWEGHYTAKADIFALGIIIWAMLER 253
Cdd:cd05074  194 LEsLADNVYTTHSDVWAFGVTMWEIMTR 221
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
112-329 7.04e-09

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 56.11  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 112 AYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML--QLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVA 189
Cdd:cd05115   75 AEALMLVMEMASGGPLNKFLSGKKDEITVSNVVELmhQVSMGMKYLEEKNFVHRDLAARNVLLVNQHY--------AKIS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 190 DFGLSKVCSASgQNPEEPVSVNKCFLStacgtdfYMAPEVWEGH-YTAKADIFALGIIIWamlERITFIDTETKKellgs 268
Cdd:cd05115  147 DFGLSKALGAD-DSYYKARSAGKWPLK-------WYAPECINFRkFSSRSDVWSYGVTMW---EAFSYGQKPYKK----- 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119628251 269 yvKQGTEIVPVGEallENPKMELlipvkKKSMNGRMKQLIKEMLAANPQDRPDAFELELRL 329
Cdd:cd05115  211 --MKGPEVMSFIE---QGKRMDC-----PAECPPEMYALMSDCWIYKWEDRPNFLTVEQRM 261
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
8-253 7.07e-09

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 55.90  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAvIRKTSARVAVKKIRchapENVELALREFwalssiksqhpnvihleecilQKDgmVQKMSHG 87
Cdd:cd05148    8 FTLERKLGSGYFGEVWEG-LWKNRVRVAIKILK----SDDLLKQQDF---------------------QKE--VQALKRL 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 SNSSLyLQLVETSLKGEiafdPrsayyLWFVMDFCDGGDMNEYLlsRKPNRKTNTSFML-----QLSSALAFLHKNQIIH 162
Cdd:cd05148   60 RHKHL-ISLFAVCSVGE----P-----VYIITELMEKGSLLAFL--RSPEGQVLPVASLidmacQVAEGMAYLEEQNSIH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEE---PVSvnkcflstacgtdfYMAPE-VWEGHYTAKA 238
Cdd:cd05148  128 RDLAARNILVGE--------DLVCKVADFGLARLIKEDVYLSSDkkiPYK--------------WTAPEaASHGTFSTKS 185
                        250
                 ....*....|....*
gi 119628251 239 DIFALGIIIWAMLER 253
Cdd:cd05148  186 DVWSFGILLYEMFTY 200
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
7-332 7.69e-09

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 55.78  E-value: 7.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSA--RVAVKKIR---CHAPEnVELALREfwALSSIKSQHPNVIHLEECILQkdgmv 81
Cdd:cd05075    1 KLALGKTLGEGEFGSVMEGQLNQDDSvlKVAVKTMKiaiCTRSE-MEDFLSE--AVCMKEFDHPNVMRLIGVCLQ----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 qkmshGSNSSLYLQLVetslkgeiafdprsayylwFVMDFCDGGDMNEYLL-SRKPNR------KTNTSFMLQLSSALAF 154
Cdd:cd05075   73 -----NTESEGYPSPV-------------------VILPFMKHGDLHSFLLySRLGDCpvylptQMLVKFMTDIASGMEY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVC-----SASGQNPEEPVSvnkcflstacgtdfYMAPE- 228
Cdd:cd05075  129 LSSKNFIHRDLAARNCMLNENM--------NVCVADFGLSKKIyngdyYRQGRISKMPVK--------------WIAIEs 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 229 VWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEivpvgealLENPkmellipvkKKSMNGrMKQLI 308
Cdd:cd05075  187 LADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNR--------LKQP---------PDCLDG-LYELM 248
                        330       340
                 ....*....|....*....|....
gi 119628251 309 KEMLAANPQDRPDAFELELRLVQI 332
Cdd:cd05075  249 SSCWLLNPKDRPSFETLRCELEKI 272
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
114-253 7.81e-09

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 55.82  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 114 YLWFVMDFCDGGDMNEYLLSRKPNRKTN--TSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdleptLKVADF 191
Cdd:cd14063   70 HLAIVTSLCKGRTLYSLIHERKEKFDFNktVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGR---------VVITDF 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 192 GLSKVcSASGQNPEEPvsvnkCFLSTACGTDFYMAPEV-------WEGH----YTAKADIFALGIIIWAMLER 253
Cdd:cd14063  141 GLFSL-SGLLQPGRRE-----DTLVIPNGWLCYLAPEIiralspdLDFEeslpFTKASDVYAFGTVWYELLAG 207
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
118-320 9.39e-09

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 55.58  E-value: 9.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH--KNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSK 195
Cdd:cd14025   71 VMEYMETGSLEKLLASEPLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILL--------DAHYHVKISDFGLAK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 196 VcsasgqnpEEPVSVNKCFLSTACGTDFYMAPEVWEGH---YTAKADIFALGIIIWAMLeritfidteTKKELLGSYVKQ 272
Cdd:cd14025  143 W--------NGLSHSHDLSRDGLRGTIAYLPPERFKEKnrcPDTKHDVYSFAIVIWGIL---------TQKKPFAGENNI 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119628251 273 GTEIVPVGEALleNPKMElLIPVKKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd14025  206 LHIMVKVVKGH--RPSLS-PIPRQRPSECQQMICLMKRCWDQDPRKRP 250
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
119-245 1.10e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 55.83  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNEYLlsrKPNRKTNTSFMLQLSSA----LAFL-HKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGL 193
Cdd:cd06649   82 MEHMDGGSLDQVL---KEAKRIPEEILGKVSIAvlrgLAYLrEKHQIMHRDVKPSNILVNS--------RGEIKLCDFGV 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119628251 194 SKVCSASGQNpeepvsvnkcflsTACGTDFYMAPEVWEG-HYTAKADIFALGI 245
Cdd:cd06649  151 SGQLIDSMAN-------------SFVGTRSYMSPERLQGtHYSVQSDIWSMGL 190
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
8-247 1.20e-08

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 55.81  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHaPENVELALREFWALSSIKSQHP---NVIHLEECilqkdgmvqkM 84
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNH-PSYARQGQIEVGILARLSNENAdefNFVRAYEC----------F 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 SHGSNSSLYLQLVETSLkgeiafdprsayylwfvMDFCDGGDMNEYLLsrkpnrKTNTSFMLQLSSALAFLHKNQIIHRD 164
Cdd:cd14229   71 QHRNHTCLVFEMLEQNL-----------------YDFLKQNKFSPLPL------KVIRPILQQVATALKKLKSLGLIHAD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 165 LKPDNILIsqtrLDTSDLEPTLKVADFGlskvcSASgqnpeepvSVNKCFLSTACGTDFYMAPEVWEG-HYTAKADIFAL 243
Cdd:cd14229  128 LKPENIML----VDPVRQPYRVKVIDFG-----SAS--------HVSKTVCSTYLQSRYYRAPEIILGlPFCEAIDMWSL 190

                 ....
gi 119628251 244 GIII 247
Cdd:cd14229  191 GCVI 194
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
147-322 1.53e-08

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 54.97  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILISQtrLDTSDlEPTLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDFYMA 226
Cdd:cd14067  122 QIAAGLAYLHKKNIIFCDLKSDNILVWS--LDVQE-HINIKLSDYGISRQSFHEGALGVE-------------GTPGYQA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 227 PEVWEG-HYTAKADIFALGIIIWAMLeritfidtETKKELLGSYVKQGTEIVPVG-EALLENPKMELLIpvkkksmngRM 304
Cdd:cd14067  186 PEIRPRiVYDEKVDMFSYGMVLYELL--------SGQRPSLGHHQLQIAKKLSKGiRPVLGQPEEVQFF---------RL 248
                        170
                 ....*....|....*...
gi 119628251 305 KQLIKEMLAANPQDRPDA 322
Cdd:cd14067  249 QALMMECWDTKPEKRPLA 266
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
147-252 1.69e-08

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 55.05  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSkVCSASGQNPEEPVsvnkcflstacGTDFYMA 226
Cdd:cd05605  110 EITCGLEHLHSERIVYRDLKPENILL--------DDHGHVRISDLGLA-VEIPEGETIRGRV-----------GTVGYMA 169
                         90       100
                 ....*....|....*....|....*..
gi 119628251 227 PEVWEGH-YTAKADIFALGIIIWAMLE 252
Cdd:cd05605  170 PEVVKNErYTFSPDWWGLGCLIYEMIE 196
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
105-195 1.78e-08

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 53.04  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 105 IAFDPRSAyylWFVMDFCDGGDMNEYLLSRKPNRKtntsFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlep 184
Cdd:COG3642   24 LDVDPDDA---DLVMEYIEGETLADLLEEGELPPE----LLRELGRLLARLHRAGIVHGDLTTSNILVDDGG-------- 88
                         90
                 ....*....|.
gi 119628251 185 tLKVADFGLSK 195
Cdd:COG3642   89 -VYLIDFGLAR 98
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
115-264 1.79e-08

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 55.45  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05627   77 LYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIaETVLAIDAIHQLGFIHRDIKPDNLLL--------DAKGHVKLSDFGL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 SKVCSASGQ---------NPEEPVSVN---------------KCFLSTACGTDFYMAPEVW-EGHYTAKADIFALGIIIW 248
Cdd:cd05627  149 CTGLKKAHRtefyrnlthNPPSDFSFQnmnskrkaetwkknrRQLAYSTVGTPDYIAPEVFmQTGYNKLCDWWSLGVIMY 228
                        170
                 ....*....|....*.
gi 119628251 249 AMLERITFIDTETKKE 264
Cdd:cd05627  229 EMLIGYPPFCSETPQE 244
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
117-329 1.87e-08

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 54.58  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 117 FVMDFCDGGDMNEYLLSRKPNRKTN-TSFMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSK 195
Cdd:cd05116   72 LVMEMAELGPLNKFLQKNRHVTEKNiTELVHQVSMGMKYLEESNFVHRDLAARNVLLVT--------QHYAKISDFGLSK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 196 VCSASgQNPEEPVSVNKCFLStacgtdfYMAPEVWEGH-YTAKADIFALGIIIWamlERITFidteTKKELLGSYVKQGT 274
Cdd:cd05116  144 ALRAD-ENYYKAQTHGKWPVK-------WYAPECMNYYkFSSKSDVWSFGVLMW---EAFSY----GQKPYKGMKGNEVT 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119628251 275 EIVPVGEAlLENPKMellIPVKkksmngrMKQLIKEMLAANPQDRPDAFELELRL 329
Cdd:cd05116  209 QMIEKGER-MECPAG---CPPE-------MYDLMKLCWTYDVDERPGFAAVELRL 252
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
12-194 2.02e-08

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 54.67  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAV---IRKTSARVAVKKIRchaPENVelalREFWALSSIKSQhpnvihleeciLQKDGMVQKMSHGS 88
Cdd:cd13981    6 KELGEGGYASVYLAKdddEQSDGSLVALKVEK---PPSI----WEFYICDQLHSR-----------LKNSRLRESISGAH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQlveTSLkgeiafdprsayylwFVMDFCD---------------GGDMNEYLLsrkpnrktnTSFMLQLSSALA 153
Cdd:cd13981   68 SAHLFQD---ESI---------------LVMDYSSqgtlldvvnkmknktGGGMDEPLA---------MFFTIELLKVVE 120
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119628251 154 FLHKNQIIHRDLKPDNILI-------SQTRLDTSDLEPTLKVADFGLS 194
Cdd:cd13981  121 ALHEVGIIHGDIKPDNFLLrleicadWPGEGENGWLSKGLKLIDFGRS 168
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
115-278 2.44e-08

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 54.26  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRK---TNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADF 191
Cdd:cd05073   80 IYIITEFMAKGSLLDFLKSDEGSKQplpKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLV--------CKIADF 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 192 GLSKVCSASGQNPEEpvsvnkcflstacGTDF---YMAPEVWE-GHYTAKADIFALGIIIWAMLE--RITF---IDTETK 262
Cdd:cd05073  152 GLARVIEDNEYTARE-------------GAKFpikWTAPEAINfGSFTIKSDVWSFGILLMEIVTygRIPYpgmSNPEVI 218
                        170
                 ....*....|....*.
gi 119628251 263 KELLGSYVKQGTEIVP 278
Cdd:cd05073  219 RALERGYRMPRPENCP 234
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
115-251 2.52e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 54.64  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP---------NR--------KTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRL 177
Cdd:cd05101  105 LYVIVEYASKGNLREYLRARRPpgmeysydiNRvpeeqmtfKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 178 dtsdleptLKVADFGLSKVCS-----ASGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05101  185 --------MKIADFGLARDINnidyyKKTTNGRLPVK--------------WMAPEaLFDRVYTHQSDVWSFGVLMWEIF 242
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
115-336 2.53e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 54.59  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP-----------------NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQtrl 177
Cdd:cd05099   93 LYVIVEYAAKGNLREFLRARRPpgpdytfditkvpeeqlSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTE--- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 178 dtsdlEPTLKVADFGLSKVCS-----ASGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05099  170 -----DNVMKIADFGLARGVHdidyyKKTSNGRLPVK--------------WMAPEaLFDRVYTHQSDVWSFGILMWEIF 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 252 EritfidtetkkelLGSYVKQGTEIVPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQDRPDAFEL--ELRL 329
Cdd:cd05099  231 T-------------LGGSPYPGIPVEELFKLLREGHRMD-----KPSNCTHELYMLMRECWHAVPTQRPTFKQLveALDK 292

                 ....*..
gi 119628251 330 VQIAFKD 336
Cdd:cd05099  293 VLAAVSE 299
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
143-251 2.61e-08

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 55.03  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKvcsaSGQNPEEPVSVNKCFLSTAcgtd 222
Cdd:cd05105  241 SFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKI--------VKICDFGLAR----DIMHDSNYVSKGSTFLPVK---- 304
                         90       100       110
                 ....*....|....*....|....*....|
gi 119628251 223 fYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05105  305 -WMAPEsIFDNLYTTLSDVWSYGILLWEIF 333
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
7-251 2.81e-08

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 54.75  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVElALREFWALSSIKSQHP----NVIHleecilqkdgMVQ 82
Cdd:cd14224   66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQ-AAEEIRILEHLKKQDKdntmNVIH----------MLE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVEtslkgeiafdprsayylwfvmdfcdggdMNEYLLSRKPNRKtntSFMLQLSSALAF-------- 154
Cdd:cd14224  135 SFTFRNHICMTFELLS----------------------------MNLYELIKKNKFQ---GFSLQLVRKFAHsilqclda 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILISQTRldtsdlEPTLKVADFGLSkvcsasgqnpeepvsvnkCF----LSTACGTDFYMAPEVW 230
Cdd:cd14224  184 LHRNKIIHCDLKPENILLKQQG------RSGIKVIDFGSS------------------CYehqrIYTYIQSRFYRAPEVI 239
                        250       260
                 ....*....|....*....|..
gi 119628251 231 EG-HYTAKADIFALGIIIWAML 251
Cdd:cd14224  240 LGaRYGMPIDMWSFGCILAELL 261
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
115-290 2.82e-08

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 54.28  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH----------KNQIIHRDLKPDNILIsQTRLdtsdlep 184
Cdd:cd14141   68 LWLITAFHEKGSLTDYLKANVVSWNELCHIAQTMARGLAYLHedipglkdghKPAIAHRDIKSKNVLL-KNNL------- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 185 TLKVADFGLSKVCSASGQNPEEPVSVnkcflstacGTDFYMAPEVWEGHYT------AKADIFALGIIIWAMLERITFID 258
Cdd:cd14141  140 TACIADFGLALKFEAGKSAGDTHGQV---------GTRRYMAPEVLEGAINfqrdafLRIDMYAMGLVLWELASRCTASD 210
                        170       180       190
                 ....*....|....*....|....*....|..
gi 119628251 259 TETKKELLgsyvkqgteivPVGEALLENPKME 290
Cdd:cd14141  211 GPVDEYML-----------PFEEEVGQHPSLE 231
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
14-248 3.24e-08

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 54.03  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAV---IRKTSA--RVAVKKIRCHAPENVELAL-REFWALSSIkSQHPNVIHLEECILQKDG----MVQK 83
Cdd:cd05054   15 LGRGAFGKVIQASafgIDKSATcrTVAVKMLKEGATASEHKALmTELKILIHI-GHHLNVVNLLGACTKPGGplmvIVEF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGsNSSLYLQLVETSLKGEIAFDPRSAYylwfVMDFCDGgdmneylLSRKPNRKTN-TSFMLQLSSALAFLHKNQIIH 162
Cdd:cd05054   94 CKFG-NLSNYLRSKREEFVPYRDKGARDVE----EEEDDDE-------LYKEPLTLEDlICYSFQVARGMEFLASRKCIH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 163 RDLKPDNILISQTRLdtsdleptLKVADFGLSK--------VCSASGQNPEEpvsvnkcflstacgtdfYMAPE-VWEGH 233
Cdd:cd05054  162 RDLAARNILLSENNV--------VKICDFGLARdiykdpdyVRKGDARLPLK-----------------WMAPEsIFDKV 216
                        250
                 ....*....|....*
gi 119628251 234 YTAKADIFALGIIIW 248
Cdd:cd05054  217 YTTQSDVWSFGVLLW 231
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-332 3.92e-08

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 53.51  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSAR---VAVKKIRchaPENVELALREFWALSSIKSQ--HPNVIHLEEcILQKDGMVqkmsh 86
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSGKeveVAVKTLK---QEHEKAGKKEFLREASVMAQldHPCIVRLIG-VCKGEPLM----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsayylwFVMDFCDGGDMNEYLLSRKP-NRKTNTSFMLQLSSALAFLHKNQIIHRDL 165
Cdd:cd05060   72 ------------------------------LVMELAPLGPLLKYLKKRREiPVSDLKELAHQVAMGMAYLESKHFVHRDL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQtrldtsdlEPTLKVADFGLSKvcsasgqnpeepvsvnkcflSTACGTDFY------------MAPE-VWEG 232
Cdd:cd05060  122 AARNVLLVN--------RHQAKISDFGMSR--------------------ALGAGSDYYrattagrwplkwYAPEcINYG 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 233 HYTAKADIFALGIIIWAMLeriTFIDTETKKellgsyvKQGTEIVpvgeALLENpkmellipvkkksmNGRMKQ------ 306
Cdd:cd05060  174 KFSSKSDVWSYGVTLWEAF---SYGAKPYGE-------MKGPEVI----AMLES--------------GERLPRpeecpq 225
                        330       340       350
                 ....*....|....*....|....*....|
gi 119628251 307 ----LIKEMLAANPQDRPDAFELELRLVQI 332
Cdd:cd05060  226 eiysIMLSCWKYRPEDRPTFSELESTFRRD 255
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
119-250 4.11e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 53.91  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 119 MDFCDGGDMNEYLlsrKPNRKTNTSFMLQLSSA----LAFL-HKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGL 193
Cdd:cd06650   82 MEHMDGGSLDQVL---KKAGRIPEQILGKVSIAvikgLTYLrEKHKIMHRDVKPSNILVNS--------RGEIKLCDFGV 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119628251 194 skvcsaSGQNPEepvSVNKCFLstacGTDFYMAPEVWEG-HYTAKADIFALGIIIWAM 250
Cdd:cd06650  151 ------SGQLID---SMANSFV----GTRSYMSPERLQGtHYSVQSDIWSMGLSLVEM 195
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
14-251 4.41e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 53.44  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIR---KTSARVAVKKIRchaPENVELALREFWALSSIKSQ--HPNVIHLEecilqkdGMVQKMSHgs 88
Cdd:cd05063   13 IGAGEFGEVFRGILKmpgRKEVAVAIKTLK---PGYTEKQRQDFLSEASIMGQfsHHNIIRLE-------GVVTKFKP-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLlsrKPNRKTNTSFML-----QLSSALAFLHKNQIIHR 163
Cdd:cd05063   81 --------------------------AMIITEYMENGALDKYL---RDHDGEFSSYQLvgmlrGIAAGMKYLSDMNYVHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 164 DLKPDNILISqtrldtSDLEptLKVADFGLSKVCSasgQNPEEPVsvnkcflsTACGTDF---YMAPE-VWEGHYTAKAD 239
Cdd:cd05063  132 DLAARNILVN------SNLE--CKVSDFGLSRVLE---DDPEGTY--------TTSGGKIpirWTAPEaIAYRKFTSASD 192
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd05063  193 VWSFGIVMWEVM 204
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
115-256 4.49e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 53.60  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLlsrkpNRKT-NTSFMLQLS----SALAFLH--------KNQIIHRDLKPDNILIsqtrldTSD 181
Cdd:cd14142   78 LWLITHYHENGSLYDYL-----QRTTlDHQEMLRLAlsaaSGLVHLHteifgtqgKPAIAHRDLKSKNILV------KSN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 182 LepTLKVADFGLSKVCSAS------GQNPEepvsvnkcflstaCGTDFYMAPEVWEGHYTA-------KADIFALGIIIW 248
Cdd:cd14142  147 G--QCCIADLGLAVTHSQEtnqldvGNNPR-------------VGTKRYMAPEVLDETINTdcfesykRVDIYAFGLVLW 211

                 ....*...
gi 119628251 249 AMLERITF 256
Cdd:cd14142  212 EVARRCVS 219
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-251 5.31e-08

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 53.50  E-value: 5.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAvirKTSARVAVK--KIRCHAPENVELALREFWALSsiKSQHPNVIhLEECILQKDGM--VQKMS 85
Cdd:cd14149   16 LSTRIGSGSFGTVYKG---KWHGDVAVKilKVVDPTPEQFQAFRNEVAVLR--KTRHVNIL-LFMGYMTKDNLaiVTQWC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  86 HGSNSSLYLQLVETSLKgeiafdprsayyLWFVMDfcdggdmneylLSRkpnrktntsfmlQLSSALAFLHKNQIIHRDL 165
Cdd:cd14149   90 EGSSLYKHLHVQETKFQ------------MFQLID-----------IAR------------QTAQGMDYLHAKNIIHRDM 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 166 KPDNILISQTRldtsdlepTLKVADFGLSKVCS--ASGQNPEEPVsvnkcflstacGTDFYMAPEVWEGH----YTAKAD 239
Cdd:cd14149  135 KSNNIFLHEGL--------TVKIGDFGLATVKSrwSGSQQVEQPT-----------GSILWMAPEVIRMQdnnpFSFQSD 195
                        250
                 ....*....|..
gi 119628251 240 IFALGIIIWAML 251
Cdd:cd14149  196 VYSYGIVLYELM 207
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
11-251 5.64e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 53.33  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREV-GRGSYGVVYEAVIRKTSAR---VAVKKIRCHAPENVElalREFWALSSIKSQ--HPNVIHLEecilqkdGMVqkm 84
Cdd:cd05065    8 IEEViGAGEFGEVCRGRLKLPGKReifVAIKTLKSGYTEKQR---RDFLSEASIMGQfdHPNIIHLE-------GVV--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgSNSSLYLQLVEtslkgeiafdprsayylwfvmdFCDGGDMNEYLlsrkpnRKTNTSF-------MLQ-LSSALAFLH 156
Cdd:cd05065   75 ---TKSRPVMIITE----------------------FMENGALDSFL------RQNDGQFtviqlvgMLRgIAAGMKYLS 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 157 KNQIIHRDLKPDNILISqtrldtSDLepTLKVADFGLSKVCSASGQNPEEpvsvnkcflSTACGTDF---YMAPE-VWEG 232
Cdd:cd05065  124 EMNYVHRDLAARNILVN------SNL--VCKVSDFGLSRFLEDDTSDPTY---------TSSLGGKIpirWTAPEaIAYR 186
                        250
                 ....*....|....*....
gi 119628251 233 HYTAKADIFALGIIIWAML 251
Cdd:cd05065  187 KFTSASDVWSYGIVMWEVM 205
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
115-320 5.85e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 53.48  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP-----------------NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRL 177
Cdd:cd05098   94 LYVIVEYASKGNLREYLQARRPpgmeycynpshnpeeqlSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 178 dtsdleptLKVADFGLSKVCS-----ASGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05098  174 --------MKIADFGLARDIHhidyyKKTTNGRLPVK--------------WMAPEaLFDRIYTHQSDVWSFGVLLWEIF 231
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 252 EritfidtetkkelLGSYVKQGTEIVPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd05098  232 T-------------LGGSPYPGVPVEELFKLLKEGHRMD-----KPSNCTNELYMMMRDCWHAVPSQRP 282
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
14-264 6.07e-08

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 53.04  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARVAVKKIrchapenvelalrefwalsSIKSQHpnvihlEECILQKDGMVQKMSHGSnsslY 93
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFV-------------------SKKMKK------KEQAAHEAALLQHLQHPQ----Y 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  94 LQLVETslkgeiaFDPRSAYYLwfVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQ-LSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd14115   52 ITLHDT-------YESPTSYIL--VLELMDDGRLLDYLMNHDELMEEKVAFYIRdIMEALQYLHNCRVAHLDIKPENLLI 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SQT----RLDTSDLEPTLKVAdfGLSKVCSASGqNPEepvsvnkcflstacgtdfYMAPEVWEG-HYTAKADIFALGIII 247
Cdd:cd14115  123 DLRipvpRVKLIDLEDAVQIS--GHRHVHHLLG-NPE------------------FAAPEVIQGtPVSLATDIWSIGVLT 181
                        250
                 ....*....|....*...
gi 119628251 248 WAMLERIT-FIDtETKKE 264
Cdd:cd14115  182 YVMLSGVSpFLD-ESKEE 198
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
7-195 6.59e-08

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 52.89  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKkirchapenvelalrefwaLSSIKSQHPNVIHLEEC--ILQKD-GMVQK 83
Cdd:cd14128    1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVK-------------------LESQKARHPQLLYESKLykILQGGvGIPHI 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGSNSS---LYLQLVETSLKGeiafdprsayylwfVMDFCdggdmneyllSRKPNRKTNTSFMLQLSSALAFLHKNQI 160
Cdd:cd14128   62 RWYGQEKDynvLVMDLLGPSLED--------------LFNFC----------SRRFTMKTVLMLADQMIGRIEYVHNKNF 117
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119628251 161 IHRDLKPDNILISQTRLDTSdleptLKVADFGLSK 195
Cdd:cd14128  118 IHRDIKPDNFLMGIGRHCNK-----LFLIDFGLAK 147
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
11-248 6.87e-08

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 53.30  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYGVVYEA-----VIRKTSARVAVKKIRCHAPENVELALREFWALSSiKSQHPNVIHL-EECILQKDgmvqkm 84
Cdd:cd05050   10 VRDIGQGAFGRVFQArapglLPYEPFTMVAVKMLKEEASADMQADFQREAALMA-EFDHPNIVKLlGVCAVGKP------ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  85 shgsnsslylqlvetslkgeiafdprsayyLWFVMDFCDGGDMNEYLLSRKPNRKTNTS--------------------- 143
Cdd:cd05050   83 ------------------------------MCLLFEYMAYGDLNEFLRHRSPRAQCSLShstssarkcglnplplscteq 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 144 --FMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSK------VCSASgQNPEEPVSvnkcfl 215
Cdd:cd05050  133 lcIAKQVAAGMAYLSERKFVHRDLATRNCLVGE--------NMVVKIADFGLSRniysadYYKAS-ENDAIPIR------ 197
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119628251 216 stacgtdfYMAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05050  198 --------WMPPEsIFYNRYTTESDVWAYGVVLW 223
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
11-193 7.20e-08

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 52.95  E-value: 7.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  11 IREVGRGSYG-VVYEAVIRKTS-ARVAVKKIRCHA-PENVELALREFWALSSIksQHPNVIhleECILQkdgmvqkmshg 87
Cdd:cd05086    2 IQEIGNGWFGkVLLGEIYTGTSvARVVVKELKASAnPKEQDDFLQQGEPYYIL--QHPNIL---QCVGQ----------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  88 snsslylqLVETslkgeiafdprsAYYLwFVMDFCDGGDMNEYLLSRKPNRKTNTSFML------QLSSALAFLHKNQII 161
Cdd:cd05086   66 --------CVEA------------IPYL-LVFEFCDLGDLKTYLANQQEKLRGDSQIMLlqrmacEIAAGLAHMHKHNFL 124
                        170       180       190
                 ....*....|....*....|....*....|..
gi 119628251 162 HRDLKPDNILIsqtrldTSDLepTLKVADFGL 193
Cdd:cd05086  125 HSDLALRNCYL------TSDL--TVKVGDYGI 148
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
115-264 8.29e-08

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 53.50  E-value: 8.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGL 193
Cdd:cd05628   76 LYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIaETVLAIDSIHQLGFIHRDIKPDNLLL--------DSKGHVKLSDFGL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 194 skvCSA--------------------------SGQNPEEPVSVNKCFLS-TACGTDFYMAPEVW-EGHYTAKADIFALGI 245
Cdd:cd05628  148 ---CTGlkkahrtefyrnlnhslpsdftfqnmNSKRKAETWKRNRRQLAfSTVGTPDYIAPEVFmQTGYNKLCDWWSLGV 224
                        170
                 ....*....|....*....
gi 119628251 246 IIWAMLERITFIDTETKKE 264
Cdd:cd05628  225 IMYEMLIGYPPFCSETPQE 243
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
8-247 1.05e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 52.84  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   8 YDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPEN----VELALreFWALSSIKSQHPNVIHLEECilqkdgmvqk 83
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYArqgqIEVSI--LSRLSQENADEFNFVRAYEC---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 MSHGSNSSLYLQLVETSL---KGEIAFDPRSAYYLwfvmdfcdggdmneyllsrKPnrktntsFMLQLSSALAFLHKNQI 160
Cdd:cd14211   69 FQHKNHTCLVFEMLEQNLydfLKQNKFSPLPLKYI-------------------RP-------ILQQVLTALLKLKSLGL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 161 IHRDLKPDNI-LISQTRldtsdlEP-TLKVADFGlskvcSASgqnpeepvSVNKCFLSTACGTDFYMAPEVWEG-HYTAK 237
Cdd:cd14211  123 IHADLKPENImLVDPVR------QPyRVKVIDFG-----SAS--------HVSKAVCSTYLQSRYYRAPEIILGlPFCEA 183
                        250
                 ....*....|
gi 119628251 238 ADIFALGIII 247
Cdd:cd14211  184 IDMWSLGCVI 193
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
4-250 1.07e-07

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 52.34  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   4 SQPKYDLIREVGRGSYGVVYEAVIR-----KTSARVAVKKIrchapeNVELALREfwalssiksqhpNVIHLEECILQKD 78
Cdd:cd05062    4 AREKITMSRELGQGSFGMVYEGIAKgvvkdEPETRVAIKTV------NEAASMRE------------RIEFLNEASVMKE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkmshgSNSSLYLQLVETSLKGEIAFdprsayylwFVMDFCDGGDMNEYLLSRKPNRKTNTSF-------MLQLS-- 149
Cdd:cd05062   66 ---------FNCHHVVRLLGVVSQGQPTL---------VIMELMTRGDLKSYLRSLRPEMENNPVQappslkkMIQMAge 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 150 --SALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSAS-----GQNPEEPVSvnkcflstacgtd 222
Cdd:cd05062  128 iaDGMAYLNANKFVHRDLAARNCMVAE--------DFTVKIGDFGMTRDIYETdyyrkGGKGLLPVR------------- 186
                        250       260
                 ....*....|....*....|....*....
gi 119628251 223 fYMAPE-VWEGHYTAKADIFALGIIIWAM 250
Cdd:cd05062  187 -WMSPEsLKDGVFTTYSDVWSFGVVLWEI 214
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
13-245 1.17e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 52.37  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  13 EVGRGSYGVVYEAVIRKTSARVAVKKIRChapENVELALREFwalssiKSQHPNVIHLEEC--ILQKDGMVqkmSHGSNS 90
Cdd:cd06616   13 EIGRGAFGTVNKMLHKPSGTIMAVKRIRS---TVDEKEQKRL------LMDLDVVMRSSDCpyIVKFYGAL---FREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  91 SLYLQLVETSLkgeiafdprSAYYLwFVMDFCDGgDMNEYLLSRkpnrktntsFMLQLSSALAFLHKN-QIIHRDLKPDN 169
Cdd:cd06616   81 WICMELMDISL---------DKFYK-YVYEVLDS-VIPEEILGK---------IAVATVKALNYLKEElKIIHRDVKPSN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 170 ILIsqtrldtsDLEPTLKVADFGLskvcsaSGQNPEepvSVNKcflSTACGTDFYMAPE------VWEGhYTAKADIFAL 243
Cdd:cd06616  141 ILL--------DRNGNIKLCDFGI------SGQLVD---SIAK---TRDAGCRPYMAPEridpsaSRDG-YDVRSDVWSL 199

                 ..
gi 119628251 244 GI 245
Cdd:cd06616  200 GI 201
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
147-251 1.31e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 52.57  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVcsasgqnpeePVsVNKCFLSTAcGTDFYMA 226
Cdd:PHA03209 165 QILEGLRYLHAQRIIHRDVKTENIFI--------NDVDQVCIGDLGAAQF----------PV-VAPAFLGLA-GTVETNA 224
                         90       100
                 ....*....|....*....|....*.
gi 119628251 227 PEVW-EGHYTAKADIFALGIIIWAML 251
Cdd:PHA03209 225 PEVLaRDKYNSKADIWSAGIVLFEML 250
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
7-251 1.45e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 52.40  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVV---YEAVIRKTsarVAVKKIRcHAPENVELALREFWALSSIKS-QHPNVIHLEECILQKdgmvQ 82
Cdd:cd07874   18 RYQNLKPIGSGAQGIVcaaYDAVLDRN---VAIKKLS-RPFQNQTHAKRAYRELVLMKCvNHKNIISLLNVFTPQ----K 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVETSLKGEIAFD---PRSAYYLWfvmdfcdggdmneyllsrkpnrktntsfmlQLSSALAFLHKNQ 159
Cdd:cd07874   90 SLEEFQDVYLVMELMDANLCQVIQMEldhERMSYLLY------------------------------QMLCGIKHLHSAG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 160 IIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASgqnpeepvsvnkcFLSTA-CGTDFYMAPEVWEGH-YTAK 237
Cdd:cd07874  140 IIHRDLKPSNIVVKS--------DCTLKILDFGLARTAGTS-------------FMMTPyVVTRYYRAPEVILGMgYKEN 198
                        250
                 ....*....|....
gi 119628251 238 ADIFALGIIIWAML 251
Cdd:cd07874  199 VDIWSVGCIMGEMV 212
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
7-195 1.60e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 51.98  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKkirchapenvelalrefwaLSSIKSQHPNvIHLEEC---ILQKDGMVQK 83
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIK-------------------LESVKTKHPQ-LLYESKlykILQGGVGIPN 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  84 M----SHGSNSSLYLQLVETSLkgEIAFDprsayylwfvmdFCdggdmneyllSRKPNRKTntSFML--QLSSALAFLHK 157
Cdd:cd14125   61 VrwygVEGDYNVMVMDLLGPSL--EDLFN------------FC----------SRKFSLKT--VLMLadQMISRIEYVHS 114
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119628251 158 NQIIHRDLKPDNILISQTRLDTsdlepTLKVADFGLSK 195
Cdd:cd14125  115 KNFIHRDIKPDNFLMGLGKKGN-----LVYIIDFGLAK 147
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
14-329 1.69e-07

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 51.97  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARV--AVKKIRCHAPENVElalREFWALSSIK---SQHPNVIHLEecilqkdGMVQKMSHgs 88
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDH---RDFAGELEVLcklGHHPNIINLL-------GACEHRGY-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nssLYLQlVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPnrktnTSFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd05047   71 ---LYLA-IEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQL-----LHFAADVARGMDYLSQKQFIHRDLAAR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTRLdtsdleptLKVADFGLSK-----VCSASGQNPEEPVSVNKCFLSTacgtdfymapevweghYTAKADIFAL 243
Cdd:cd05047  142 NILVGENYV--------AKIADFGLSRgqevyVKKTMGRLPVRWMAIESLNYSV----------------YTTNSDVWSY 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 244 GIIIWAMLEritfidtetkkelLGSYVKQGTEIVPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQDRPDAF 323
Cdd:cd05047  198 GVLLWEIVS-------------LGGTPYCGMTCAELYEKLPQGYRLE-----KPLNCDDEVYDLMRQCWREKPYERPSFA 259

                 ....*.
gi 119628251 324 ELELRL 329
Cdd:cd05047  260 QILVSL 265
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
7-251 1.92e-07

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 51.93  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIRE-------VGRGSYGVVYEAV---IRK--TSARVAVKKIRCHAPENVELAL-REFWALSSIkSQHPNVIHLEEC 73
Cdd:cd14207    1 KWEFARErlklgksLGRGAFGKVVQASafgIKKspTCRVVAVKMLKEGATASEYKALmTELKILIHI-GHHLNVVNLLGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  74 ILQKDG----MVQKMSHGSNSS-------LYLQLVETSLKGEIAFDPRSA-------YYLWFVMD---FCDGGDMNEYLL 132
Cdd:cd14207   80 CTKSGGplmvIVEYCKYGNLSNylkskrdFFVTNKDTSLQEELIKEKKEAeptggkkKRLESVTSsesFASSGFQEDKSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 133 SRKPNRKTNT--------------SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCS 198
Cdd:cd14207  160 SDVEEEEEDSgdfykrpltmedliSYSFQVARGMEFLSSRKCIHRDLAARNILLSENNV--------VKICDFGLARDIY 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119628251 199 asgQNPEEpVSVNKCFLSTAcgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd14207  232 ---KNPDY-VRKGDARLPLK-----WMAPEsIFDKIYSTKSDVWSYGVLLWEIF 276
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
34-274 2.01e-07

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 51.92  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  34 VAVKKIRCHAPENVELA-LREFWALSSIKSqhPNVIHLeecilqkdgmvqkmshgsnsslylqlvetsLKGEIAFDPrsa 112
Cdd:cd05095   49 VAVKMLRADANKNARNDfLKEIKIMSRLKD--PNIIRL------------------------------LAVCITDDP--- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 113 yyLWFVMDFCDGGDMNEYLLSRKPNRK------------TNTSFM-LQLSSALAFLHKNQIIHRDLKPDNILISQTRldt 179
Cdd:cd05095   94 --LCMITEYMENGDLNQFLSRQQPEGQlalpsnaltvsySDLRFMaAQIASGMKYLSSLNFVHRDLATRNCLVGKNY--- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 180 sdlepTLKVADFGLSKVCSASgqnpeepvsvnkcflstacgtDFY------MAPEVWE-------GHYTAKADIFALGII 246
Cdd:cd05095  169 -----TIKIADFGMSRNLYSG---------------------DYYriqgraVLPIRWMswesillGKFTTASDVWAFGVT 222
                        250       260
                 ....*....|....*....|....*...
gi 119628251 247 IWamlERITFIDTETKKELLGSYVKQGT 274
Cdd:cd05095  223 LW---ETLTFCREQPYSQLSDEQVIENT 247
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7-250 2.02e-07

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 51.94  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPenvelalreFWALSSIKsqhpnvIHLEECILQKDG----MVQ 82
Cdd:cd14226   14 RYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKA---------FLNQAQIE------VRLLELMNKHDTenkyYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  83 KMSHGSNSSLYLQLVetslkgeiaFDPRSayylwfvmdfcdggdMNEYLLSRKPN---------RKtntsFMLQLSSALA 153
Cdd:cd14226   79 RLKRHFMFRNHLCLV---------FELLS---------------YNLYDLLRNTNfrgvslnltRK----FAQQLCTALL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 154 FLHKN--QIIHRDLKPDNILISQTRLDtsdlepTLKVADFGLSkvcsasgqnpeepvsvnkCFLSTA----CGTDFYMAP 227
Cdd:cd14226  131 FLSTPelSIIHCDLKPENILLCNPKRS------AIKIIDFGSS------------------CQLGQRiyqyIQSRFYRSP 186
                        250       260
                 ....*....|....*....|....
gi 119628251 228 EVWEG-HYTAKADIFALGIIIWAM 250
Cdd:cd14226  187 EVLLGlPYDLAIDMWSLGCILVEM 210
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
1-247 2.59e-07

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 51.63  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   1 MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHA--PENVELALREFWALSSIKSQHPNVIHLEECilqkd 78
Cdd:cd14227   10 LCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPsyARQGQIEVSILARLSTESADDYNFVRAYEC----- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  79 gmvqkMSHGSNSSLYLQLVETSLKG---EIAFDPRSAYYLWFVMDfcdggdmneyllsrkpnrktntsfmlQLSSALAFL 155
Cdd:cd14227   85 -----FQHKNHTCLVFEMLEQNLYDflkQNKFSPLPLKYIRPILQ--------------------------QVATALMKL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 156 HKNQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGlskvcSASgqnpeepvSVNKCFLSTACGTDFYMAPEVWEG-HY 234
Cdd:cd14227  134 KSLGLIHADLKPENIML----VDPSRQPYRVKVIDFG-----SAS--------HVSKAVCSTYLQSRYYRAPEIILGlPF 196
                        250
                 ....*....|...
gi 119628251 235 TAKADIFALGIII 247
Cdd:cd14227  197 CEAIDMWSLGCVI 209
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
34-251 3.14e-07

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 51.09  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  34 VAVKKIRCHAPENVELA-LREFWALSSIKSqhPNVIHLEECILQKDGmvqkmshgsnsslylqlvetslkgeiafdprsa 112
Cdd:cd05096   49 VAVKILRPDANKNARNDfLKEVKILSRLKD--PNIIRLLGVCVDEDP--------------------------------- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 113 yyLWFVMDFCDGGDMNEYLLSRKPNRKTNTS--------------------FMLQLSSALAFLHKNQIIHRDLKPDNILI 172
Cdd:cd05096   94 --LCMITEYMENGDLNQFLSSHHLDDKEENGndavppahclpaisyssllhVALQIASGMKYLSSLNFVHRDLATRNCLV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 173 SQTRldtsdlepTLKVADFGLSKVCSASgqnpeepvsvnkcflstacgtDFY------------MApevWE----GHYTA 236
Cdd:cd05096  172 GENL--------TIKIADFGMSRNLYAG---------------------DYYriqgravlpirwMA---WEcilmGKFTT 219
                        250
                 ....*....|....*
gi 119628251 237 KADIFALGIIIWAML 251
Cdd:cd05096  220 ASDVWAFGVTLWEIL 234
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
10-248 3.17e-07

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 51.02  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  10 LIREVGRGSYGVVYEAVIRkTSARVAVKKIRchapenvELALREfwalssiksqhpnvihleECILQKDGMVQKMSHGSN 89
Cdd:cd05114    8 FMKELGSGLFGVVRLGKWR-AQYKVAIKAIR-------EGAMSE------------------EDFIEEAKVMMKLTHPKL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  90 SSLYLqlVETSLKGeiafdprsayyLWFVMDFCDGGDMNEYLLSRKP--NRKTNTSFMLQLSSALAFLHKNQIIHRDLKP 167
Cdd:cd05114   62 VQLYG--VCTQQKP-----------IYIVTEFMENGCLLNYLRQRRGklSRDMLLSMCQDVCEGMEYLERNNFIHRDLAA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 168 DNILISQTRldtsdlepTLKVADFGLSKVCSasgqnPEEPVSvnkcflstACGTDF---YMAPEVWE-GHYTAKADIFAL 243
Cdd:cd05114  129 RNCLVNDTG--------VVKVSDFGMTRYVL-----DDQYTS--------SSGAKFpvkWSPPEVFNySKFSSKSDVWSF 187

                 ....*
gi 119628251 244 GIIIW 248
Cdd:cd05114  188 GVLMW 192
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
118-251 3.47e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 50.78  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 118 VMDFCDGGDMNEYLLSRKPNRKTNTS------------------FMLQLSSALAFLHKNQIIHRDLKPDNILISQtrldt 179
Cdd:cd05090   85 LFEFMNQGDLHEFLIMRSPHSDVGCSsdedgtvkssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILVGE----- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119628251 180 sdlEPTLKVADFGLSKVCSASGQNPEEPvsvnKCFLSTAcgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05090  160 ---QLHVKISDLGLSREIYSSDYYRVQN----KSLLPIR-----WMPPEaIMYGKFSSDSDIWSFGVVLWEIF 220
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
14-332 3.72e-07

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 50.77  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRKTSARV--AVKKIRCHAPENVElalREFWALSSIK---SQHPNVIHLeecilqkdgmvqkMSHGS 88
Cdd:cd05089   10 IGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDH---RDFAGELEVLcklGHHPNIINL-------------LGACE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRktntsFMLQLSSALAFLHKNQIIHRDLKPD 168
Cdd:cd05089   74 NRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAKEHGTASTLTSQQLLQ-----FASDVAKGMQYLSEKQFIHRDLAAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILISQTRLDtsdleptlKVADFGLSKvcsasgqnpEEPVSVNKCFLSTACGtdfYMAPEVWE-GHYTAKADIFALGIII 247
Cdd:cd05089  149 NVLVGENLVS--------KIADFGLSR---------GEEVYVKKTMGRLPVR---WMAIESLNySVYTTKSDVWSFGVLL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 248 WAMLEritfidtetkkelLGSYVKQGTEIVPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQDRPDAFELEL 327
Cdd:cd05089  209 WEIVS-------------LGGTPYCGMTCAELYEKLPQGYRME-----KPRNCDDEVYELMRQCWRDRPYERPPFSQISV 270

                 ....*
gi 119628251 328 RLVQI 332
Cdd:cd05089  271 QLSRM 275
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
1-247 4.10e-07

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 51.24  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   1 MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHaPENVELALREFWALSSIKSQHP---NVIHLEECilqk 77
Cdd:cd14228   10 LCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNH-PSYARQGQIEVSILSRLSSENAdeyNFVRSYEC---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  78 dgmvqkMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVmdfcdggdmneyllsrKPnrktntsFMLQLSSALAFLHK 157
Cdd:cd14228   85 ------FQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYI----------------RP-------ILQQVATALMKLKS 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 158 NQIIHRDLKPDNILIsqtrLDTSDLEPTLKVADFGlskvcSASgqnpeepvSVNKCFLSTACGTDFYMAPEVWEG-HYTA 236
Cdd:cd14228  136 LGLIHADLKPENIML----VDPVRQPYRVKVIDFG-----SAS--------HVSKAVCSTYLQSRYYRAPEIILGlPFCE 198
                        250
                 ....*....|.
gi 119628251 237 KADIFALGIII 247
Cdd:cd14228  199 AIDMWSLGCVI 209
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
115-320 4.11e-07

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 51.17  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKP-----------------NRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQtrl 177
Cdd:cd05100   93 LYVLVEYASKGNLREYLRARRPpgmdysfdtcklpeeqlTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTE--- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 178 dtsdlEPTLKVADFGLSKVCS-----ASGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05100  170 -----DNVMKIADFGLARDVHnidyyKKTTNGRLPVK--------------WMAPEaLFDRVYTHQSDVWSFGVLLWEIF 230
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119628251 252 EritfidtetkkelLGSYVKQGTEIVPVGEALLENPKMEllipvKKKSMNGRMKQLIKEMLAANPQDRP 320
Cdd:cd05100  231 T-------------LGGSPYPGIPVEELFKLLKEGHRMD-----KPANCTHELYMIMRECWHAVPSQRP 281
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
143-248 4.32e-07

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 51.06  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKVCSASGQ-----NPEEPVSvnkcflst 217
Cdd:cd05104  218 SFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRI--------TKICDFGLARDIRNDSNyvvkgNARLPVK-------- 281
                         90       100       110
                 ....*....|....*....|....*....|..
gi 119628251 218 acgtdfYMAPE-VWEGHYTAKADIFALGIIIW 248
Cdd:cd05104  282 ------WMAPEsIFECVYTFESDVWSYGILLW 307
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
144-251 4.36e-07

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 51.16  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 144 FMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSKvcsaSGQNPEEPVSVNKCFLSTAcgtdf 223
Cdd:cd05107  244 FSYQVANGMEFLASKNCVHRDLAARNVLICEGKL--------VKICDFGLAR----DIMRDSNYISKGSTFLPLK----- 306
                         90       100
                 ....*....|....*....|....*....
gi 119628251 224 YMAPE-VWEGHYTAKADIFALGIIIWAML 251
Cdd:cd05107  307 WMAPEsIFNNLYTTLSDVWSFGILLWEIF 335
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
12-252 4.52e-07

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 50.74  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSARVAVKKI---RCHAPENVELALREFWALSSIKSQHpnVIHLEECILQKDGMVQKMSHGS 88
Cdd:cd05632    8 RVLGKGGFGEVCACQVRATGKMYACKRLekkRIKKRKGESMALNEKQILEKVNSQF--VVNLAYAYETKDALCLVLTIMN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 NSSLYLQLVETslkGEIAFDPRSAyyLWFVMDFCDGgdmneyllsrkpnrktntsfmlqlssaLAFLHKNQIIHRDLKPD 168
Cdd:cd05632   86 GGDLKFHIYNM---GNPGFEEERA--LFYAAEILCG---------------------------LEDLHRENTVYRDLKPE 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 169 NILIsqtrldtsDLEPTLKVADFGLSKvcsasgQNPEEPVsvnkcfLSTACGTDFYMAPEVWEGH-YTAKADIFALGIII 247
Cdd:cd05632  134 NILL--------DDYGHIRISDLGLAV------KIPEGES------IRGRVGTVGYMAPEVLNNQrYTLSPDYWGLGCLI 193

                 ....*
gi 119628251 248 WAMLE 252
Cdd:cd05632  194 YEMIE 198
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
147-247 4.53e-07

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 50.27  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLHKNQIIHRDLKPDNILISQTRldtsdlepTLKVADFGLSKVCSASGQNPEEpvsvnkcflstacGTDF--- 223
Cdd:cd05067  111 QIAEGMAFIEERNYIHRDLRAANILVSDTL--------SCKIADFGLARLIEDNEYTARE-------------GAKFpik 169
                         90       100
                 ....*....|....*....|....*
gi 119628251 224 YMAPEVWE-GHYTAKADIFALGIII 247
Cdd:cd05067  170 WTAPEAINyGTFTIKSDVWSFGILL 194
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
34-293 4.96e-07

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 50.74  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  34 VAVKKIRCHAPENVELA-LREFWALSSIKsqHPNVIHLEeCILQKDgmvqkmshgsnsslylqlvetslkgeiafDPrsa 112
Cdd:cd05097   47 VAVKMLRADVTKTARNDfLKEIKIMSRLK--NPNIIRLL-GVCVSD-----------------------------DP--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 113 yyLWFVMDFCDGGDMNEYLLSRKPNRK------------TNTSFM-LQLSSALAFLHKNQIIHRDLKPDNILISQTRldt 179
Cdd:cd05097   92 --LCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMaVQIASGMKYLASLNFVHRDLATRNCLVGNHY--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 180 sdlepTLKVADFGLSKVCSASgqnpeepvsvnkcflstacgtDFY------------MApevWE----GHYTAKADIFAL 243
Cdd:cd05097  167 -----TIKIADFGMSRNLYSG---------------------DYYriqgravlpirwMA---WEsillGKFTTASDVWAF 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119628251 244 GIIIWAML-----ERITFIDTETKKELLGSYVK-QGTEIVPVGEALLENPKMELLI 293
Cdd:cd05097  218 GVTLWEMFtlckeQPYSLLSDEQVIENTGEFFRnQGRQIYLSQTPLCPSPVFKLMM 273
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
120-281 5.36e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 50.26  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 120 DFCDGGDMNEYllsRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISqTRldtsdlePTLKVADFGLSKVCSA 199
Cdd:cd06619   79 EFMDGGSLDVY---RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVN-TR-------GQVKLCDFGVSTQLVN 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 200 SgqnpeepvsvnkcFLSTACGTDFYMAPEVWEG-HYTAKADIFALGIIIWAM-LERITFIDTETKK------ELLGSYVK 271
Cdd:cd06619  148 S-------------IAKTYVGTNAYMAPERISGeQYGIHSDVWSLGISFMELaLGRFPYPQIQKNQgslmplQLLQCIVD 214
                        170
                 ....*....|
gi 119628251 272 QGTEIVPVGE 281
Cdd:cd06619  215 EDPPVLPVGQ 224
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
143-251 6.72e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 50.43  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFML-QLSSALAFLHKNQIIHRDLKPDNILISQtrldtsdlEPTLKVADFGLSKVCSASGQNPEEPVsvnkcflstacgT 221
Cdd:cd07875  129 SYLLyQMLCGIKHLHSAGIIHRDLKPSNIVVKS--------DCTLKILDFGLARTAGTSFMMTPYVV------------T 188
                         90       100       110
                 ....*....|....*....|....*....|.
gi 119628251 222 DFYMAPEVWEGH-YTAKADIFALGIIIWAML 251
Cdd:cd07875  189 RYYRAPEVILGMgYKENVDIWSVGCIMGEMI 219
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
151-322 8.31e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 49.93  E-value: 8.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 151 ALAFLHKNQIIHRDLKPDNILISQTrldtsdlEPTLKVADFGLSkvcSASGQNPEEPVSvnkcflstacgTDFYMAPEV- 229
Cdd:cd14020  122 ALAFLHHEGYVHADLKPRNILWSAE-------DECFKLIDFGLS---FKEGNQDVKYIQ-----------TDGYRAPEAe 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 230 -----------WEGHYTAKADIFALGIIIWAMLERITFIDTETKKEllgsYVKQGTEIVP--VGEALLENPKmellIPVK 296
Cdd:cd14020  181 lqnclaqaglqSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSQE----WKDNSSAIIDhiFASNAVVNPA----IPAY 252
                        170       180
                 ....*....|....*....|....*.
gi 119628251 297 kksmngRMKQLIKEMLAANPQDRPDA 322
Cdd:cd14020  253 ------HLRDLIKSMLHNDPGKRATA 272
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
115-253 8.33e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 50.05  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 115 LWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLH--------KNQIIHRDLKPDNILISQTrldtsdlePTL 186
Cdd:cd14219   78 LYLITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHteifstqgKPAIAHRDLKSKNILVKKN--------GTC 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119628251 187 KVADFGLSKVCSASGQNPEEPvsvnkcfLSTACGTDFYMAPEVWE-----GHYTA--KADIFALGIIIWAMLER 253
Cdd:cd14219  150 CIADLGLAVKFISDTNEVDIP-------PNTRVGTKRYMPPEVLDeslnrNHFQSyiMADMYSFGLILWEVARR 216
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
147-251 8.45e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 49.88  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 147 QLSSALAFLH-KNQIIHRDLKPDNILISQTRLDtsdleptLKVADFGlskvcsasgqnpeepvsvnkcflsTACGTD--F 223
Cdd:cd14136  127 QVLQGLDYLHtKCGIIHTDIKPENVLLCISKIE-------VKIADLG------------------------NACWTDkhF 175
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119628251 224 --------YMAPEVWEG-HYTAKADIFALGIIIWAML 251
Cdd:cd14136  176 tediqtrqYRSPEVILGaGYGTPADIWSTACMAFELA 212
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
14-253 1.04e-06

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 49.55  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  14 VGRGSYGVVYEAVIRK---TSARVAVK--KIRCHAPENVELALREFWALSSIksQHPNVIHLEecilqkdGMVQKMShgs 88
Cdd:cd14204   15 LGEGEFGSVMEGELQQpdgTNHKVAVKtmKLDNFSQREIEEFLSEAACMKDF--NHPNVIRLL-------GVCLEVG--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  89 nsslylqlvetslkgeiafdPRSAYYLWFVMDFCDGGDMNEYLLSRKPNR-------KTNTSFMLQLSSALAFLHKNQII 161
Cdd:cd14204   83 --------------------SQRIPKPMVILPFMKYGDLHSFLLRSRLGSgpqhvplQTLLKFMIDIALGMEYLSSRNFL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILIsqtRLDTsdlepTLKVADFGLSKVCSA-----SGQNPEEPVSvnkcflstacgtdfYMAPE-VWEGHYT 235
Cdd:cd14204  143 HRDLAARNCML---RDDM-----TVCVADFGLSKKIYSgdyyrQGRIAKMPVK--------------WIAVEsLADRVYT 200
                        250
                 ....*....|....*...
gi 119628251 236 AKADIFALGIIIWAMLER 253
Cdd:cd14204  201 VKSDVWAFGVTMWEIATR 218
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
150-245 1.04e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 49.68  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 150 SALAFL-HKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSASGQNpeepvsvnkcflSTACGTDFYMAPE 228
Cdd:cd06618  125 KALHYLkEKHGVIHRDVKPSNILL--------DESGNVKLCDFGISGRLVDSKAK------------TRSAGCAAYMAPE 184
                         90       100
                 ....*....|....*....|.
gi 119628251 229 VWE----GHYTAKADIFALGI 245
Cdd:cd06618  185 RIDppdnPKYDIRADVWSLGI 205
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
125-327 1.06e-06

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 49.11  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 125 GDMNEYLLSRKPNRKTNTSFML-QLSSALAFLHKNQIIHRDLKpdnilisQTRLDTSDLEPTlKVADFGLSKVCSASGQN 203
Cdd:cd14024   69 GDMHSHVRRRRRLSEDEARGLFtQMARAVAHCHQHGVILRDLK-------LRRFVFTDELRT-KLVLVNLEDSCPLNGDD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 204 PEepvsvnkcfLSTACGTDFYMAPEVW-EGH-YTAK-ADIFALGIIIWAMLE-RITFIDTETKkeLLGSYVKQGTEIVPV 279
Cdd:cd14024  141 DS---------LTDKHGCPAYVGPEILsSRRsYSGKaADVWSLGVCLYTMLLgRYPFQDTEPA--ALFAKIRRGAFSLPA 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119628251 280 GeallenpkmellipvkkksMNGRMKQLIKEMLAANPQDRPDAFELEL 327
Cdd:cd14024  210 W-------------------LSPGARCLVSCMLRRSPAERLKASEILL 238
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
12-251 1.07e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 49.48  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  12 REVGRGSYGVVYEAVIRKTSAR---VAVKKIRCHAPENVElalREFWALSSIKSQ--HPNVIHLEecilqkdGMVQKmsh 86
Cdd:cd05066   10 KVIGAGEFGEVCSGRLKLPGKReipVAIKTLKAGYTEKQR---RDFLSEASIMGQfdHPNIIHLE-------GVVTR--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  87 gsnsslylqlvetslkgeiafdprsAYYLWFVMDFCDGGDMNEYLlsrkpnRKTNTSF-------MLQ-LSSALAFLHKN 158
Cdd:cd05066   77 -------------------------SKPVMIVTEYMENGSLDAFL------RKHDGQFtviqlvgMLRgIASGMKYLSDM 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 159 QIIHRDLKPDNILISqtrldtSDLepTLKVADFGLSKVCSasgQNPEEPVsvnkcflsTACGTDF---YMAPE-VWEGHY 234
Cdd:cd05066  126 GYVHRDLAARNILVN------SNL--VCKVSDFGLSRVLE---DDPEAAY--------TTRGGKIpirWTAPEaIAYRKF 186
                        250
                 ....*....|....*..
gi 119628251 235 TAKADIFALGIIIWAML 251
Cdd:cd05066  187 TSASDVWSYGIVMWEVM 203
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
143-250 1.07e-06

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 49.37  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFMLQLSSALAFLHKNQIIHRDLKPDNILIsqtrldtsDLEPTLKVADFGLSKVCSAS-----GQNPEEPVSvnkcflst 217
Cdd:cd05043  120 HMALQIACGMSYLHRRGVIHKDIAARNCVI--------DDELQVKITDNALSRDLFPMdyhclGDNENRPIK-------- 183
                         90       100       110
                 ....*....|....*....|....*....|....
gi 119628251 218 acgtdfYMAPEVWEG-HYTAKADIFALGIIIWAM 250
Cdd:cd05043  184 ------WMSLESLVNkEYSSASDVWSFGVLLWEL 211
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
155-325 1.67e-06

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 48.94  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 155 LHKNQIIHRDLKPDNILISQ-TRLDTsdleptlkVADFGLSKVCSASGQNpeepvsvnkcfLSTACGTDFYMAPEVWEGH 233
Cdd:cd13974  148 LHKKNIVHRDLKLGNMVLNKrTRKIT--------ITNFCLGKHLVSEDDL-----------LKDQRGSPAYISPDVLSGK 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 234 -YTAKA-DIFALGIIIWAML-ERITFIDTeTKKELLGSyVKQGTEIVPVGEALLENpkmellipvkkksmngrMKQLIKE 310
Cdd:cd13974  209 pYLGKPsDMWALGVVLFTMLyGQFPFYDS-IPQELFRK-IKAAEYTIPEDGRVSEN-----------------TVCLIRK 269
                        170
                 ....*....|....*
gi 119628251 311 MLAANPQDRPDAFEL 325
Cdd:cd13974  270 LLVLNPQKRLTASEV 284
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
143-250 2.17e-06

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 49.07  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 143 SFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLdtsdleptLKVADFGLSK-VCSASGQ----NPEEPVSvnkcflst 217
Cdd:cd05106  216 RFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRV--------AKICDFGLARdIMNDSNYvvkgNARLPVK-------- 279
                         90       100       110
                 ....*....|....*....|....*....|....
gi 119628251 218 acgtdfYMAPE-VWEGHYTAKADIFALGIIIWAM 250
Cdd:cd05106  280 ------WMAPEsIFDCVYTVQSDVWSYGILLWEI 307
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
7-266 2.39e-06

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 48.69  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251   7 KYDLIREVGRGSYGVVYEAV-IRKTSARVAVKKIRchapeNV----ELALREFWALSSIKSQHPNVIHleECIlqkdGMV 81
Cdd:cd14213   13 RYEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVK-----NVdryrEAARSEIQVLEHLNTTDPNSTF--RCV----QML 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251  82 QKMSHGSNSSLYLQLVETSLKGEIafdpRSAYYLWFVMDFCdggdmneyllsrkpnrktnTSFMLQLSSALAFLHKNQII 161
Cdd:cd14213   82 EWFDHHGHVCIVFELLGLSTYDFI----KENSFLPFPIDHI-------------------RNMAYQICKSVNFLHHNKLT 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119628251 162 HRDLKPDNILISQT-----------RLDTSDLEPTLKVADFGlskvcSASGQNPEEpvsvnkcflSTACGTDFYMAPEV- 229
Cdd:cd14213  139 HTDLKPENILFVQSdyvvkynpkmkRDERTLKNPDIKVVDFG-----SATYDDEHH---------STLVSTRHYRAPEVi 204
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119628251 230 WEGHYTAKADIFALGIIIWAMLERITFIDTETKKELL 266
Cdd:cd14213  205 LALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHL 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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